ID 3MG1_ECOLI Reviewed; 187 AA. AC P05100; Q2M7L0; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 16-DEC-2009, entry version 87. DE RecName: Full=DNA-3-methyladenine glycosylase 1; DE EC=3.2.2.20; DE AltName: Full=DNA-3-methyladenine glycosylase I; DE AltName: Full=3-methyladenine-DNA glycosylase I, constitutive; DE Short=TAG I; DE AltName: Full=DNA-3-methyladenine glycosidase I; GN Name=tag; OrderedLocusNames=b3549, JW3518; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-29. RX MEDLINE=87057218; PubMed=3536912; RA Sakumi K., Nakabeppu Y., Yamamoto Y., Kawabata S., Iwanaga S., RA Sekiguchi M.; RT "Purification and structure of 3-methyladenine-DNA glycosylase I of RT Escherichia coli."; RL J. Biol. Chem. 261:15761-15766(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=86232617; PubMed=3520491; DOI=10.1093/nar/14.9.3763; RA Steinum A.-L., Seeberg E.; RT "Nucleotide sequence of the tag gene from Escherichia coli."; RL Nucleic Acids Res. 14:3763-3772(1986). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=94316500; PubMed=8041620; DOI=10.1093/nar/22.13.2576; RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.; RT "Analysis of the Escherichia coli genome. V. DNA sequence of the RT region from 76.0 to 81.5 minutes."; RL Nucleic Acids Res. 22:2576-2586(1994). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [6] RP STRUCTURE BY NMR. RX PubMed=12161745; DOI=10.1038/nsb829; RA Drohat A.C., Kwon K., Krosky D.J., Stivers J.T.; RT "3-Methyladenine DNA glycosylase I is an unexpected helix-hairpin- RT helix superfamily member."; RL Nat. Struct. Biol. 9:659-664(2002). RN [7] RP STRUCTURE BY NMR, AND ZINC-BINDING SITES. RX PubMed=12654914; DOI=10.1074/jbc.M300934200; RA Kwon K., Cao C., Stivers J.T.; RT "A novel zinc snap motif conveys structural stability to 3- RT methyladenine DNA glycosylase I."; RL J. Biol. Chem. 278:19442-19446(2003). RN [8] RP STRUCTURE BY NMR IN COMPLEX WITH 3-METHYLADENINE, AND ZINC-BINDING RP SITES. RX PubMed=13129925; DOI=10.1074/jbc.M307500200; RA Cao C., Kwon K., Jiang Y.L., Drohat A.C., Stivers J.T.; RT "Solution structure and base perturbation studies reveal a novel mode RT of alkylated base recognition by 3-methyladenine DNA glycosylase I."; RL J. Biol. Chem. 278:48012-48020(2003). CC -!- FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to CC excise 3-methyladenine from the damaged DNA polymer formed by CC alkylation lesions. CC -!- CATALYTIC ACTIVITY: Hydrolysis of alkylated DNA, releasing 3- CC methyladenine. CC -!- ENZYME REGULATION: Activity is controlled by product inhibition. CC -!- INTERACTION: CC P0AFG8:aceE; NbExp=1; IntAct=EBI-558722, EBI-542683; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J02606; AAA24658.1; -; Genomic_DNA. DR EMBL; X03845; CAA27472.1; -; Genomic_DNA. DR EMBL; U00039; AAB18526.1; -; Genomic_DNA. DR EMBL; U00096; AAC76573.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77746.1; -; Genomic_DNA. DR PIR; A24604; DGECM1. DR RefSeq; AP_004245.1; -. DR RefSeq; NP_418005.1; -. DR PDB; 1LMZ; NMR; -; A=1-187. DR PDB; 1NKU; NMR; -; A=1-187. DR PDB; 1P7M; NMR; -; A=1-187. DR PDBsum; 1LMZ; -. DR PDBsum; 1NKU; -. DR PDBsum; 1P7M; -. DR DIP; DIP-10950N; -. DR IntAct; P05100; 4. DR STRING; P05100; -. DR ECO2DBASE; H021.1; 6TH EDITION. DR GeneID; 947137; -. DR GenomeReviews; AP009048_GR; JW3518. DR GenomeReviews; U00096_GR; b3549. DR KEGG; ecj:JW3518; -. DR KEGG; eco:b3549; -. DR EchoBASE; EB0979; -. DR EcoGene; EG10986; tag. DR HOGENOM; HBG747469; -. DR OMA; YVAYHDT; -. DR BioCyc; EcoCyc:EG10986-MON; -. DR BioCyc; ECOL168927:B3549-MON; -. DR Genevestigator; P05100; -. DR GO; GO:0008725; F:DNA-3-methyladenine glycosylase I activity; IEA:EC. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0006284; P:base-excision repair; IEA:InterPro. DR InterPro; IPR005019; Adenine_glyco. DR InterPro; IPR011257; DNA_glycosylase. DR InterPro; IPR004597; Tag. DR Pfam; PF03352; Adenine_glyco; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; KW DNA damage; DNA repair; Hydrolase; Metal-binding; Zinc. FT CHAIN 1 187 DNA-3-methyladenine glycosylase 1. FT /FTId=PRO_0000194877. FT METAL 4 4 Zinc. FT METAL 17 17 Zinc. FT METAL 175 175 Zinc. FT METAL 179 179 Zinc. FT HELIX 11 19 FT STRAND 20 23 FT HELIX 28 41 FT HELIX 46 60 FT TURN 61 63 FT HELIX 65 69 FT HELIX 73 80 FT HELIX 89 107 FT HELIX 112 119 FT TURN 120 122 FT HELIX 132 134 FT HELIX 140 152 FT HELIX 159 169 FT STRAND 171 173 FT STRAND 177 181 SQ SEQUENCE 187 AA; 21100 MW; 5A305B5CA66A48FE CRC64; MERCGWVSQD PLYIAYHDNE WGVPETDSKK LFEMICLEGQ QAGLSWITVL KKRENYRACF HQFDPVKVAA MQEEDVERLV QDAGIIRHRG KIQAIIGNAR AYLQMEQNGE PFVDFVWSFV NHQPQVTQAT TLSEIPTSTS ASDALSKALK KRGFKFVGTT ICYSFMQACG LVNDHVVGCC CYPGNKP // ID 3MG2_ECOLI Reviewed; 282 AA. AC P04395; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-1987, sequence version 1. DT 15-DEC-2009, entry version 99. DE RecName: Full=DNA-3-methyladenine glycosylase 2; DE EC=3.2.2.21; DE AltName: Full=DNA-3-methyladenine glycosylase II; DE AltName: Full=3-methyladenine-DNA glycosylase II, inducible; DE Short=TAG II; DE AltName: Full=DNA-3-methyladenine glycosidase II; GN Name=alkA; Synonyms=aidA; OrderedLocusNames=b2068, JW2053; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-12 AND RP 14-20. RX MEDLINE=85054800; PubMed=6094528; RA Nakabeppu Y., Miyata T., Kondo H., Iwanaga S., Sekiguchi M.; RT "Structure and expression of the alkA gene of Escherichia coli RT involved in adaptive response to alkylating agents."; RL J. Biol. Chem. 259:13730-13736(1984). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX MEDLINE=97251358; PubMed=9097040; DOI=10.1093/dnares/3.6.379; RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., RA Yamamoto Y., Horiuchi T.; RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome RT corresponding to the 40.1-50.0 min region on the linkage map."; RL DNA Res. 3:379-392(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP CHARACTERIZATION. RX MEDLINE=85054799; PubMed=6389535; RA Nakabeppu Y., Kondo H., Sekiguchi M.; RT "Cloning and characterization of the alkA gene of Escherichia coli RT that encodes 3-methyladenine DNA glycosylase II."; RL J. Biol. Chem. 259:13723-13729(1984). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-2. RX MEDLINE=86313568; PubMed=3529081; DOI=10.1073/pnas.83.17.6297; RA Nakabeppu Y., Sekiguchi M.; RT "Regulatory mechanisms for induction of synthesis of repair enzymes in RT response to alkylating agents: ada protein acts as a transcriptional RT regulator."; RL Proc. Natl. Acad. Sci. U.S.A. 83:6297-6301(1986). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND MUTAGENESIS. RX MEDLINE=96319733; PubMed=8706135; DOI=10.1016/S0092-8674(00)80102-6; RA Yamagata Y., Kato M., Odawara K., Tokuno Y., Nakashima Y., RA Matsushima N., Yasumura K., Tomita K., Ihara K., Fujii Y., RA Nakabeppu Y., Sekiguchi M., Fujii S.; RT "Three-dimensional structure of a DNA repair enzyme, 3-methyladenine RT DNA glycosylase II, from Escherichia coli."; RL Cell 86:311-319(1996). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RX MEDLINE=96319734; PubMed=8706136; DOI=10.1016/S0092-8674(00)80103-8; RA Labahn J., Scharer O.D., Long A., Ezaz-Nikpay K., Verdine G.L., RA Ellenberger T.E.; RT "Structural basis for the excision repair of alkylation-damaged DNA."; RL Cell 86:321-329(1996). CC -!- FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to CC excise 3-methyladenine, 3-methylguanine, 7-methylguanine, O2- CC methylthymine, and O2-methylcytosine from the damaged DNA polymer CC formed by alkylation lesions. CC -!- CATALYTIC ACTIVITY: Hydrolysis of alkylated DNA, releasing 3- CC methyladenine, 3-methylguanine, 7-methylguanine and 7- CC methyladenine. CC -!- SUBUNIT: Monomer. CC -!- INTERACTION: CC P06959:aceF; NbExp=1; IntAct=EBI-544077, EBI-542707; CC -!- INDUCTION: When E.coli cells are exposed to doses of DNA CC alkylating agent. It is not inhibited by reaction products. CC -!- SIMILARITY: Belongs to the alkylbase DNA glycosidase alkA family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; K02498; AAA23430.1; -; Genomic_DNA. DR EMBL; U00096; AAC75129.1; -; Genomic_DNA. DR EMBL; AP009048; BAA15926.1; -; Genomic_DNA. DR EMBL; M13827; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A00904; DGECMA. DR RefSeq; AP_002668.1; -. DR RefSeq; NP_416572.1; -. DR PDB; 1DIZ; X-ray; 2.50 A; A/B=1-282. DR PDB; 1MPG; X-ray; 1.80 A; A/B=1-282. DR PDB; 1PVS; X-ray; 2.40 A; A/B=1-282. DR PDB; 3CVS; X-ray; 2.40 A; A/B/C/D=1-282. DR PDB; 3CVT; X-ray; 2.50 A; A/B/C/D=1-282. DR PDB; 3CW7; X-ray; 2.30 A; A/B/C/D=1-282. DR PDB; 3CWA; X-ray; 2.40 A; A/B/C/D=1-282. DR PDB; 3CWS; X-ray; 2.30 A; A/B/C/D=1-282. DR PDB; 3CWT; X-ray; 2.30 A; A/B/C/D=1-282. DR PDB; 3CWU; X-ray; 2.80 A; A/B/C/D=1-282. DR PDB; 3D4V; X-ray; 2.90 A; A/B/C/D=1-282. DR PDBsum; 1DIZ; -. DR PDBsum; 1MPG; -. DR PDBsum; 1PVS; -. DR PDBsum; 3CVS; -. DR PDBsum; 3CVT; -. DR PDBsum; 3CW7; -. DR PDBsum; 3CWA; -. DR PDBsum; 3CWS; -. DR PDBsum; 3CWT; -. DR PDBsum; 3CWU; -. DR PDBsum; 3D4V; -. DR DIP; DIP-9084N; -. DR IntAct; P04395; 19. DR STRING; P04395; -. DR GeneID; 947371; -. DR GenomeReviews; AP009048_GR; JW2053. DR GenomeReviews; U00096_GR; b2068. DR KEGG; ecj:JW2053; -. DR KEGG; eco:b2068; -. DR EchoBASE; EB1204; -. DR EcoGene; EG11222; alkA. DR HOGENOM; HBG510250; -. DR OMA; LHIWYTD; -. DR BioCyc; EcoCyc:EG11222-MON; -. DR BioCyc; ECOL168927:B2068-MON; -. DR Genevestigator; P04395; -. DR GO; GO:0003905; F:alkylbase DNA N-glycosylase activity; IEA:EC. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0006284; P:base-excision repair; IEA:InterPro. DR InterPro; IPR010316; AlkA_N. DR InterPro; IPR000035; Alkylbase_DNA_glycsylse_CS. DR InterPro; IPR011257; DNA_glycosylase. DR InterPro; IPR003265; HhH-GPD_domain. DR InterPro; IPR012294; TFIID_C/glycos_N. DR Gene3D; G3DSA:3.30.310.20; AlkA_N; 1. DR Pfam; PF06029; AlkA_N; 1. DR Pfam; PF00730; HhH-GPD; 1. DR SMART; SM00478; ENDO3c; 1. DR PROSITE; PS00516; ALKYLBASE_DNA_GLYCOS; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; KW DNA damage; DNA repair; Hydrolase. FT CHAIN 1 282 DNA-3-methyladenine glycosylase 2. FT /FTId=PRO_0000194878. FT ACT_SITE 238 238 Proton acceptor. FT SITE 218 218 Determinant for substrate specificity FT and/or activity. FT MUTAGEN 124 124 Q->A: Methylmethane sulfonate-resistant. FT MUTAGEN 218 218 W->A: No catalytic activity, FT methylmethane sulfonate-sensitive. FT MUTAGEN 237 237 D->N: More than 30% catalytic activity, FT methylmethane sulfonate-resistant. FT MUTAGEN 238 238 D->N: No catalytic activity, FT methylmethane sulfonate-sensitive. FT STRAND 2 5 FT HELIX 12 22 FT TURN 25 27 FT STRAND 28 30 FT STRAND 35 41 FT STRAND 44 53 FT TURN 54 57 FT STRAND 58 63 FT HELIX 65 70 FT HELIX 71 82 FT TURN 83 85 FT HELIX 88 95 FT HELIX 96 99 FT HELIX 113 122 FT TURN 123 125 FT HELIX 128 142 FT HELIX 158 162 FT HELIX 166 171 FT HELIX 176 190 FT HELIX 202 209 FT HELIX 217 227 FT HELIX 239 244 FT HELIX 250 257 FT HELIX 258 260 FT HELIX 264 272 SQ SEQUENCE 282 AA; 31393 MW; B66BB5E23019899C CRC64; MYTLNWQPPY DWSWMLGFLA ARAVSSVETV ADSYYARSLA VGEYRGVVTA IPDIARHTLH INLSAGLEPV AAECLAKMSR LFDLQCNPQI VNGALGRLGA ARPGLRLPGC VDAFEQGVRA ILGQLVSVAM AAKLTARVAQ LYGERLDDFP EYICFPTPQR LAAADPQALK ALGMPLKRAE ALIHLANAAL EGTLPMTIPG DVEQAMKTLQ TFPGIGRWTA NYFALRGWQA KDVFLPDDYL IKQRFPGMTP AQIRRYAERW KPWRSYALLH IWYTEGWQPD EA // ID 6PGD_ECOLI Reviewed; 468 AA. AC P00350; P78080; Q47571; Q59366; Q59402; Q59411; Q59412; Q59413; AC Q59414; Q59416; Q79DT3; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 15-DEC-2009, entry version 90. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating; DE EC=1.1.1.44; GN Name=gnd; OrderedLocusNames=b2029, JW2011; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=84237540; PubMed=6329905; DOI=10.1016/0378-1119(84)90070-2; RA Nasoff M.S., Baker H.V. II, Wolf R.E. Jr.; RT "DNA sequence of the Escherichia coli gene, gnd, for 6- RT phosphogluconate dehydrogenase."; RL Gene 27:253-264(1984). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ECOR 10; RX MEDLINE=91267957; PubMed=2050640; RA Bisercic M., Feutrier J.Y., Reeves P.R.; RT "Nucleotide sequences of the gnd genes from nine natural isolates of RT Escherichia coli: evidence of intragenic recombination as a RT contributing factor in the evolution of the polymorphic gnd locus."; RL J. Bacteriol. 173:3894-3900(1991). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ECOR 45, ECOR 65, ECOR 67, ECOR 68, ECOR 69, and ECOR 70; RX MEDLINE=92041624; PubMed=1938920; RA Dykhuizen D.E., Green L.; RT "Recombination in Escherichia coli and the definition of biological RT species."; RL J. Bacteriol. 173:7257-7268(1991). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX MEDLINE=97251358; PubMed=9097040; DOI=10.1093/dnares/3.6.379; RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., RA Yamamoto Y., Horiuchi T.; RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome RT corresponding to the 40.1-50.0 min region on the linkage map."; RL DNA Res. 3:379-392(1996). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125. RX MEDLINE=89126937; PubMed=2464736; RA Miller R.D., Dykhuizen D.E., Hartl D.L.; RT "Fitness effects of a deletion mutation increasing transcription of RT the 6-phosphogluconate dehydrogenase gene in Escherichia coli."; RL Mol. Biol. Evol. 5:691-703(1988). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125. RX MEDLINE=88086897; PubMed=3275621; RA Barcak G.J., Wolf R.E. Jr.; RT "Comparative nucleotide sequence analysis of growth-rate-regulated gnd RT alleles from natural isolates of Escherichia coli and from Salmonella RT typhimurium LT-2."; RL J. Bacteriol. 170:372-379(1988). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125. RC STRAIN=O7:K1 / VW187; RX MEDLINE=93106949; PubMed=7677991; RA Marolda C.L., Valvano M.A.; RT "Identification, expression, and DNA sequence of the GDP-mannose RT biosynthesis genes encoded by the O7 rfb gene cluster of strain VW187 RT (Escherichia coli O7:K1)."; RL J. Bacteriol. 175:148-158(1993). CC -!- CATALYTIC ACTIVITY: 6-phospho-D-gluconate + NADP(+) = D-ribulose CC 5-phosphate + CO(2) + NADPH. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 3/3. CC -!- INTERACTION: CC P18843:nadE; NbExp=1; IntAct=EBI-907049, EBI-548960; CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; K02072; AAA23918.1; -; Genomic_DNA. DR EMBL; M63821; AAA24488.1; -; Genomic_DNA. DR EMBL; M64326; AAA24204.1; -; Genomic_DNA. DR EMBL; M64327; AAA24205.1; -; Genomic_DNA. DR EMBL; M64328; AAA24206.1; -; Genomic_DNA. DR EMBL; M64329; AAA24207.1; -; Genomic_DNA. DR EMBL; M64330; AAA24208.1; -; Genomic_DNA. DR EMBL; M64331; AAA24209.1; -; Genomic_DNA. DR EMBL; U00096; AAC75090.1; -; Genomic_DNA. DR EMBL; AP009048; BAA15869.1; -; Genomic_DNA. DR EMBL; M23181; AAA23924.1; -; Genomic_DNA. DR EMBL; M18956; AAA23919.1; -; Genomic_DNA. DR EMBL; M18957; AAA23920.1; -; Genomic_DNA. DR EMBL; M18960; AAA23922.1; -; Genomic_DNA. DR EMBL; AF125322; AAC27540.1; -; Genomic_DNA. DR PIR; D64968; DEECGC. DR PIR; I62463; I62463. DR PIR; I62465; I62465. DR RefSeq; AP_002630.1; -. DR RefSeq; NP_416533.1; -. DR PDB; 2ZYA; X-ray; 1.60 A; A/B=1-468. DR PDB; 2ZYD; X-ray; 1.50 A; A/B=1-468. DR PDB; 3FWN; X-ray; 1.50 A; A/B=1-468. DR PDBsum; 2ZYA; -. DR PDBsum; 2ZYD; -. DR PDBsum; 3FWN; -. DR IntAct; P00350; 5. DR ECO2DBASE; C042.6; 6TH EDITION. DR PRIDE; P00350; -. DR GeneID; 946554; -. DR GenomeReviews; AP009048_GR; JW2011. DR GenomeReviews; U00096_GR; b2029. DR KEGG; ecj:JW2011; -. DR KEGG; eco:b2029; -. DR EchoBASE; EB0406; -. DR EcoGene; EG10411; gnd. DR OMA; GQKEAYD; -. DR BioCyc; EcoCyc:6PGLUCONDEHYDROG-MON; -. DR BioCyc; ECOL168927:B2029-MON; -. DR BioCyc; MetaCyc:6PGLUCONDEHYDROG-MON; -. DR Genevestigator; P00350; -. DR GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxyla...; IEA:EC. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-KW. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR006183; 6-phosphogluconate_DH. DR InterPro; IPR006114; 6PGDH_C. DR InterPro; IPR006113; 6PGDH_decarbox. DR InterPro; IPR006115; 6PGDH_NAD-bd. DR InterPro; IPR006184; 6PGdom_BS. DR InterPro; IPR013328; DH_multihelical. DR InterPro; IPR012284; Fibritin/6PGD_C-extension. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:1.20.5.320; Fibritin/6PGD_C-extension; 1. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Gene3D; G3DSA:1.10.1040.10; Opine_DH; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR PROSITE; PS00461; 6PGD; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Gluconate utilization; NADP; KW Oxidoreductase; Pentose shunt. FT CHAIN 1 468 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090037. FT VARIANT 2 2 S -> L (in strain: ECOR 70). FT VARIANT 32 32 F -> Y (in strain: ECOR 70). FT VARIANT 39 39 T -> Q (in strain: O7:K1 / VW187). FT VARIANT 52 52 V -> D (in strain: ECOR 10). FT VARIANT 55 55 Y -> F (in strain: ECOR 10). FT VARIANT 102 102 N -> K (in strain: ECOR 65). FT VARIANT 117 117 A -> S (in strain: ECOR 70). FT VARIANT 123 125 IGT -> YRY (in strain: O7:K1 / VW187). FT VARIANT 170 170 V -> F (in strain: ECOR 10). FT VARIANT 175 175 A -> S (in strain: ECOR 45). FT VARIANT 209 209 N -> S (in strain: ECOR 68). FT VARIANT 211 211 T -> S (in strain: ECOR 10 and ECOR 69). FT VARIANT 216 216 A -> T (in strain: ECOR 67). FT VARIANT 294 294 D -> E (in strain: ECOR 70). FT VARIANT 308 308 A -> G (in strain: ECOR 68). FT VARIANT 313 313 D -> N (in strain: ECOR 67). FT VARIANT 315 315 A -> G (in strain: ECOR 70). FT VARIANT 325 325 L -> Q (in strain: ECOR 69). FT VARIANT 330 330 I -> S (in strain: ECOR 10). FT VARIANT 350 350 D -> A (in strain: ECOR 10 and ECOR 69). FT VARIANT 369 369 Q -> R (in strain: ECOR 10). FT VARIANT 422 422 S -> A (in strain: ECOR 10, ECOR 65, ECOR FT 68, ECOR 69 and ECOR 70). FT CONFLICT 306 306 P -> R (in Ref. 1; AAA23918). SQ SEQUENCE 468 AA; 51481 MW; 62A32C84DC596D86 CRC64; MSKQQIGVVG MAVMGRNLAL NIESRGYTVS IFNRSREKTE EVIAENPGKK LVPYYTVKEF VESLETPRRI LLMVKAGAGT DAAIDSLKPY LDKGDIIIDG GNTFFQDTIR RNRELSAEGF NFIGTGVSGG EEGALKGPSI MPGGQKEAYE LVAPILTKIA AVAEDGEPCV TYIGADGAGH YVKMVHNGIE YGDMQLIAEA YSLLKGGLNL TNEELAQTFT EWNNGELSSY LIDITKDIFT KKDEDGNYLV DVILDEAANK GTGKWTSQSA LDLGEPLSLI TESVFARYIS SLKDQRVAAS KVLSGPQAQP AGDKAEFIEK VRRALYLGKI VSYAQGFSQL RAASEEYNWD LNYGEIAKIF RAGCIIRAQF LQKITDAYAE NPQIANLLLA PYFKQIADDY QQALRDVVAY AVQNGIPVPT FSAAVAYYDS YRAAVLPANL IQAQRDYFGA HTYKRIDKEG VFHTEWLD // ID 6PGL_ECOLI Reviewed; 331 AA. AC P52697; P75760; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 15-DEC-2009, entry version 75. DE RecName: Full=6-phosphogluconolactonase; DE Short=6-P-gluconolactonase; DE Short=Pgl; DE EC=3.1.1.31; GN Name=pgl; Synonyms=ybhE; OrderedLocusNames=b0767, JW0750; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX MEDLINE=95394784; PubMed=7665460; RA Maupin-Furlow J.A., Rosentel J.K., Lee J.H., Deppenmeier U., RA Gunsalus R.P., Shanmugam K.T.; RT "Genetic analysis of the modABCD (molybdate transport) operon of RT Escherichia coli."; RL J. Bacteriol. 177:4851-4856(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX MEDLINE=97061202; PubMed=8905232; DOI=10.1093/dnares/3.3.137; RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., RA Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., RA Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., RA Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., RA Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., RA Yano M., Horiuchi T.; RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome RT corresponding to the 12.7-28.0 min region on the linkage map."; RL DNA Res. 3:137-155(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP IDENTIFICATION. RA Rudd K.E.; RL Unpublished observations (MAR-1996). RN [6] RP FUNCTION. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=15576773; DOI=10.1128/JB.186.24.8248-8253.2004; RA Thomason L.C., Court D.L., Datta A.R., Khanna R., Rosner J.L.; RT "Identification of the Escherichia coli K-12 ybhE gene as pgl, RT encoding 6-phosphogluconolactonase."; RL J. Bacteriol. 186:8248-8253(2004). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-287, AND MASS SPECTROMETRY. RX PubMed=18723842; DOI=10.1074/mcp.M800187-MCP200; RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., RA Grishin N.V., Zhao Y.; RT "Lysine acetylation is a highly abundant and evolutionarily conserved RT modification in Escherichia coli."; RL Mol. Cell. Proteomics 8:215-225(2009). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RA Lima C.D., Kniewel R., Solorzano V., Wu J.; RT "Structure of a putative 7-bladed propeller isomerase."; RL Submitted (NOV-2003) to the PDB data bank. CC -!- FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to CC 6-phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2/3. CC -!- SIMILARITY: Belongs to the cycloisomerase 2 family. CC -!- SEQUENCE CAUTION: CC Sequence=U27192; Type=Frameshift; Positions=110; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U27192; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; U00096; AAC73854.1; -; Genomic_DNA. DR EMBL; AP009048; BAA35431.1; -; Genomic_DNA. DR PIR; G64812; G64812. DR RefSeq; AP_001398.1; -. DR RefSeq; NP_415288.1; -. DR PDB; 1RI6; X-ray; 2.00 A; A=2-331. DR PDBsum; 1RI6; -. DR STRING; P52697; -. DR 2DBase-Ecoli; P52697; -. DR GeneID; 946398; -. DR GenomeReviews; AP009048_GR; JW0750. DR GenomeReviews; U00096_GR; b0767. DR KEGG; ecj:JW0750; -. DR KEGG; eco:b0767; -. DR EchoBASE; EB3020; -. DR EcoGene; EG13231; pgl. DR HOGENOM; HBG741123; -. DR OMA; EGCHSAN; -. DR BioCyc; EcoCyc:6PGLUCONOLACT-MON; -. DR BioCyc; ECOL168927:B0767-MON; -. DR BioCyc; MetaCyc:6PGLUCONOLACT-MON; -. DR Genevestigator; P52697; -. DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:HAMAP. DR GO; GO:0006006; P:glucose metabolic process; IEA:HAMAP. DR HAMAP; MF_01605; -; 1. DR InterPro; IPR019405; DUF2394. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom. DR Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1. DR Pfam; PF10282; DUF2394; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Carbohydrate metabolism; Complete proteome; KW Glucose metabolism; Hydrolase. FT CHAIN 1 331 6-phosphogluconolactonase. FT /FTId=PRO_0000171132. FT MOD_RES 287 287 N6-acetyllysine. FT CONFLICT 37 52 QVQPMVVSPDKRYLYV -> RCSRWWSARTNVISML (in FT Ref. 1). FT CONFLICT 319 331 VGQGPMWVVVNAH -> SGRDQCGWWLTHTKR (in Ref. FT 1). FT STRAND 2 9 FT HELIX 10 12 FT STRAND 14 20 FT STRAND 26 33 FT STRAND 41 43 FT STRAND 47 54 FT TURN 55 58 FT STRAND 59 65 FT TURN 67 69 FT STRAND 72 79 FT STRAND 85 89 FT STRAND 93 100 FT TURN 101 104 FT STRAND 105 112 FT STRAND 115 123 FT STRAND 138 145 FT HELIX 146 148 FT STRAND 150 156 FT STRAND 162 171 FT STRAND 178 183 FT STRAND 187 194 FT TURN 195 198 FT STRAND 199 206 FT STRAND 213 219 FT STRAND 231 236 FT STRAND 240 247 FT TURN 248 251 FT STRAND 252 258 FT STRAND 265 272 FT STRAND 274 276 FT STRAND 280 282 FT STRAND 286 292 FT TURN 294 296 FT STRAND 298 305 FT TURN 306 309 FT STRAND 310 318 FT STRAND 320 322 SQ SEQUENCE 331 AA; 36308 MW; D731044CFCF31A8F CRC64; MKQTVYIASP ESQQIHVWNL NHEGALTLTQ VVDVPGQVQP MVVSPDKRYL YVGVRPEFRV LAYRIAPDDG ALTFAAESAL PGSPTHISTD HQGQFVFVGS YNAGNVSVTR LEDGLPVGVV DVVEGLDGCH SANISPDNRT LWVPALKQDR ICLFTVSDDG HLVAQDPAEV TTVEGAGPRH MVFHPNEQYA YCVNELNSSV DVWELKDPHG NIECVQTLDM MPENFSDTRW AADIHITPDG RHLYACDRTA SLITVFSVSE DGSVLSKEGF QPTETQPRGF NVDHSGKYLI AAGQKSHHIS VYEIVGEQGL LHEKGRYAVG QGPMWVVVNA H //