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Database: UniProt/SWISS-PROT
Entry: GLPD_ECOLI
LinkDB: GLPD_ECOLI
Original site: GLPD_ECOLI 
ID   GLPD_ECOLI              Reviewed;         501 AA.
AC   P13035; P78115; Q2M790; Q47234;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 3.
DT   25-OCT-2017, entry version 160.
DE   RecName: Full=Aerobic glycerol-3-phosphate dehydrogenase;
DE            EC=1.1.5.3;
GN   Name=glpD; Synonyms=glyD; OrderedLocusNames=b3426, JW3389;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=1987111; DOI=10.1128/jb.173.1.101-107.1991;
RA   Austin D., Larson T.J.;
RT   "Nucleotide sequence of the glpD gene encoding aerobic sn-glycerol 3-
RT   phosphate dehydrogenase of Escherichia coli K-12.";
RL   J. Bacteriol. 173:101-107(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Choi Y.-L., Kawase S., Kawamukai M., Utsumi R., Sakai H., Komano T.;
RT   "Nucleotide sequence of the glycerol-3-phosphate dehydrogenase gene of
RT   Escherichia coli and regulation by the cAMP-CRP complex.";
RL   Agric. Biol. Chem. 53:1135-1143(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   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 277:1453-1462(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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61.
RC   STRAIN=K12;
RX   PubMed=3045087; DOI=10.1128/jb.170.9.4209-4215.1988;
RA   Ye S., Larson T.J.;
RT   "Structures of the promoter and operator of the glpD gene encoding
RT   aerobic sn-glycerol-3-phosphate dehydrogenase of Escherichia coli K-
RT   12.";
RL   J. Bacteriol. 170:4209-4215(1988).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61.
RX   PubMed=3045764; DOI=10.1093/nar/16.15.7732;
RA   Choi Y.-L., Kawase S., Nishida T., Sakai H., Komano T., Kawamukai M.,
RA   Utsumi R., Kohara Y., Akiyama K.;
RT   "Nucleotide sequence of the glpR gene encoding the repressor for the
RT   glycerol-3-phosphate regulon of Escherichia coli K12.";
RL   Nucleic Acids Res. 16:7732-7732(1988).
RN   [7]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
RA   Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
CC   -!- FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone.
CC       Uses molecular oxygen or nitrate as electron acceptor.
CC   -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + a quinone =
CC       glycerone phosphate + a quinol.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol
CC       kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate
CC       (aerobic route): step 1/1.
CC   -!- INTERACTION:
CC       P0AEE8:dam; NbExp=3; IntAct=EBI-548509, EBI-548491;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: There are two sn-glycerol-3-phosphate dehydrogenase
CC       isozymes in E.coli: one is aerobic, the other anaerobic.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA23888.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; M55989; AAA24636.1; -; Genomic_DNA.
DR   EMBL; M96795; AAC28164.1; -; Genomic_DNA.
DR   EMBL; D00425; BAA00327.1; -; Genomic_DNA.
DR   EMBL; U18997; AAA58224.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76451.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77866.1; -; Genomic_DNA.
DR   EMBL; M21277; AAA23885.1; -; Genomic_DNA.
DR   EMBL; M54940; AAA23888.1; ALT_INIT; Genomic_DNA.
DR   PIR; A39186; DEECGD.
DR   RefSeq; NP_417884.1; NC_000913.3.
DR   RefSeq; WP_000448136.1; NZ_LN832404.1.
DR   PDB; 2QCU; X-ray; 1.75 A; A/B=1-501.
DR   PDB; 2R45; X-ray; 2.30 A; A/B=1-501.
DR   PDB; 2R46; X-ray; 2.10 A; A/B=1-501.
DR   PDB; 2R4E; X-ray; 2.10 A; A/B=1-501.
DR   PDB; 2R4J; X-ray; 1.96 A; A/B=1-501.
DR   PDBsum; 2QCU; -.
DR   PDBsum; 2R45; -.
DR   PDBsum; 2R46; -.
DR   PDBsum; 2R4E; -.
DR   PDBsum; 2R4J; -.
DR   ProteinModelPortal; P13035; -.
DR   SMR; P13035; -.
DR   BioGrid; 4261265; 401.
DR   DIP; DIP-9793N; -.
DR   IntAct; P13035; 91.
DR   MINT; MINT-1248675; -.
DR   STRING; 316385.ECDH10B_3600; -.
DR   SWISS-2DPAGE; P13035; -.
DR   PaxDb; P13035; -.
DR   PRIDE; P13035; -.
DR   EnsemblBacteria; AAC76451; AAC76451; b3426.
DR   EnsemblBacteria; BAE77866; BAE77866; BAE77866.
DR   GeneID; 947934; -.
DR   KEGG; ecj:JW3389; -.
DR   KEGG; eco:b3426; -.
DR   PATRIC; fig|511145.12.peg.3521; -.
DR   EchoBASE; EB0389; -.
DR   EcoGene; EG10394; glpD.
DR   eggNOG; ENOG4105C6V; Bacteria.
DR   eggNOG; COG0578; LUCA.
DR   HOGENOM; HOG000004811; -.
DR   InParanoid; P13035; -.
DR   KO; K00111; -.
DR   PhylomeDB; P13035; -.
DR   BioCyc; EcoCyc:AERGLYC3PDEHYDROG-MONOMER; -.
DR   BioCyc; MetaCyc:AERGLYC3PDEHYDROG-MONOMER; -.
DR   BRENDA; 1.1.1.94; 2026.
DR   UniPathway; UPA00618; UER00674.
DR   EvolutionaryTrace; P13035; -.
DR   PRO; PR:P13035; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IDA:EcoCyc.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR   GO; GO:0009055; F:electron carrier activity; IDA:EcoCyc.
DR   GO; GO:0071949; F:FAD binding; IDA:EcoCyc.
DR   GO; GO:0052590; F:sn-glycerol-3-phosphate:ubiquinone oxidoreductase activity; IDA:EcoCyc.
DR   GO; GO:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IMP:EcoCyc.
DR   InterPro; IPR031656; DAO_C.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000447; G3P_DH_FAD-dep.
DR   PANTHER; PTHR11985; PTHR11985; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16901; DAO_C; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF51905; SSF51905; 2.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
DR   PROSITE; PS00978; FAD_G3PDH_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Cytoplasm; FAD; Flavoprotein;
KW   Glycerol metabolism; Oxidoreductase; Reference proteome.
FT   CHAIN         1    501       Aerobic glycerol-3-phosphate
FT                                dehydrogenase.
FT                                /FTId=PRO_0000126098.
FT   NP_BIND       5     33       FAD. {ECO:0000255}.
FT   CONFLICT     23     23       A -> G (in Ref. 2; BAA00327).
FT                                {ECO:0000305}.
FT   CONFLICT    328    353       QAITRDYTLDIHDENGKAPLLSVFGG -> HVLPVITPLIF
FT                                MMKMAKHRCCRYSAA (in Ref. 2; BAA00327).
FT                                {ECO:0000305}.
FT   CONFLICT    464    501       DDALWRRTKQGMWLNADQQSRVSQWLVEYTQQRLSLAS ->
FT                                ARRPVASHKTRHVAKCGSTISCESVAGGVYAAEVIAGVVN
FT                                (in Ref. 2; BAA00327). {ECO:0000305}.
FT   STRAND        4      9       {ECO:0000244|PDB:2QCU}.
FT   HELIX        13     24       {ECO:0000244|PDB:2QCU}.
FT   STRAND       29     32       {ECO:0000244|PDB:2QCU}.
FT   STRAND       34     36       {ECO:0000244|PDB:2QCU}.
FT   HELIX        41     43       {ECO:0000244|PDB:2QCU}.
FT   HELIX        53     58       {ECO:0000244|PDB:2QCU}.
FT   HELIX        61     77       {ECO:0000244|PDB:2QCU}.
FT   TURN         79     81       {ECO:0000244|PDB:2QCU}.
FT   STRAND       82     90       {ECO:0000244|PDB:2QCU}.
FT   TURN         93     95       {ECO:0000244|PDB:2QCU}.
FT   HELIX        98    109       {ECO:0000244|PDB:2QCU}.
FT   STRAND      110    112       {ECO:0000244|PDB:2QCU}.
FT   STRAND      115    117       {ECO:0000244|PDB:2QCU}.
FT   STRAND      121    124       {ECO:0000244|PDB:2QCU}.
FT   STRAND      129    131       {ECO:0000244|PDB:2QCU}.
FT   STRAND      137    146       {ECO:0000244|PDB:2QCU}.
FT   HELIX       148    161       {ECO:0000244|PDB:2QCU}.
FT   STRAND      165    167       {ECO:0000244|PDB:2QCU}.
FT   STRAND      169    178       {ECO:0000244|PDB:2QCU}.
FT   STRAND      181    188       {ECO:0000244|PDB:2QCU}.
FT   TURN        189    191       {ECO:0000244|PDB:2QCU}.
FT   STRAND      194    200       {ECO:0000244|PDB:2QCU}.
FT   STRAND      202    204       {ECO:0000244|PDB:2QCU}.
FT   HELIX       207    209       {ECO:0000244|PDB:2QCU}.
FT   HELIX       210    216       {ECO:0000244|PDB:2QCU}.
FT   STRAND      229    237       {ECO:0000244|PDB:2QCU}.
FT   STRAND      239    241       {ECO:0000244|PDB:2QCU}.
FT   STRAND      245    249       {ECO:0000244|PDB:2QCU}.
FT   STRAND      255    261       {ECO:0000244|PDB:2QCU}.
FT   TURN        262    264       {ECO:0000244|PDB:2QCU}.
FT   STRAND      265    269       {ECO:0000244|PDB:2QCU}.
FT   HELIX       279    281       {ECO:0000244|PDB:2QCU}.
FT   HELIX       286    299       {ECO:0000244|PDB:2QCU}.
FT   STRAND      300    302       {ECO:0000244|PDB:2QCU}.
FT   HELIX       306    308       {ECO:0000244|PDB:2QCU}.
FT   STRAND      311    317       {ECO:0000244|PDB:2QCU}.
FT   HELIX       327    329       {ECO:0000244|PDB:2QCU}.
FT   STRAND      335    341       {ECO:0000244|PDB:2QCU}.
FT   STRAND      344    351       {ECO:0000244|PDB:2QCU}.
FT   HELIX       355    357       {ECO:0000244|PDB:2QCU}.
FT   HELIX       358    369       {ECO:0000244|PDB:2QCU}.
FT   HELIX       370    372       {ECO:0000244|PDB:2QCU}.
FT   HELIX       381    383       {ECO:0000244|PDB:2QCU}.
FT   STRAND      391    393       {ECO:0000244|PDB:2QCU}.
FT   TURN        394    397       {ECO:0000244|PDB:2QCU}.
FT   HELIX       398    405       {ECO:0000244|PDB:2QCU}.
FT   HELIX       411    420       {ECO:0000244|PDB:2QCU}.
FT   HELIX       422    424       {ECO:0000244|PDB:2QCU}.
FT   HELIX       425    429       {ECO:0000244|PDB:2QCU}.
FT   HELIX       435    438       {ECO:0000244|PDB:2QCU}.
FT   HELIX       448    457       {ECO:0000244|PDB:2QCU}.
FT   HELIX       463    468       {ECO:0000244|PDB:2QCU}.
FT   HELIX       473    475       {ECO:0000244|PDB:2QCU}.
FT   HELIX       479    494       {ECO:0000244|PDB:2QCU}.
FT   STRAND      495    498       {ECO:0000244|PDB:2QCU}.
SQ   SEQUENCE   501 AA;  56751 MW;  1C4D341E9E4536AB CRC64;
     METKDLIVIG GGINGAGIAA DAAGRGLSVL MLEAQDLACA TSSASSKLIH GGLRYLEHYE
     FRLVSEALAE REVLLKMAPH IAFPMRFRLP HRPHLRPAWM IRIGLFMYDH LGKRTSLPGS
     TGLRFGANSV LKPEIKRGFE YSDCWVDDAR LVLANAQMVV RKGGEVLTRT RATSARRENG
     LWIVEAEDID TGKKYSWQAR GLVNATGPWV KQFFDDGMHL PSPYGIRLIK GSHIVVPRVH
     TQKQAYILQN EDKRIVFVIP WMDEFSIIGT TDVEYKGDPK AVKIEESEIN YLLNVYNTHF
     KKQLSRDDIV WTYSGVRPLC DDESDSPQAI TRDYTLDIHD ENGKAPLLSV FGGKLTTYRK
     LAEHALEKLT PYYQGIGPAW TKESVLPGGA IEGDRDDYAA RLRRRYPFLT ESLARHYART
     YGSNSELLLG NAGTVSDLGE DFGHEFYEAE LKYLVDHEWV RRADDALWRR TKQGMWLNAD
     QQSRVSQWLV EYTQQRLSLA S
//
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