GenomeNet

Database: UniProt/SWISS-PROT
Entry: GLPA_ECOLI
LinkDB: GLPA_ECOLI
Original site: GLPA_ECOLI 
ID   GLPA_ECOLI              Reviewed;         542 AA.
AC   P0A9C0; P13032; P78238;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   13-FEB-2019, entry version 113.
DE   RecName: Full=Anaerobic glycerol-3-phosphate dehydrogenase subunit A;
DE            Short=G-3-P dehydrogenase;
DE            EC=1.1.5.3;
GN   Name=glpA; OrderedLocusNames=b2241, JW2235;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
RC   STRAIN=K12;
RX   PubMed=3286606; DOI=10.1128/jb.170.6.2448-2456.1988;
RA   Cole S.T., Eiglmeier K., Ahmed S., Honore N., Elmes L., Anderson W.F.,
RA   Weiner J.H.;
RT   "Nucleotide sequence and gene-polypeptide relationships of the glpABC
RT   operon encoding the anaerobic sn-glycerol-3-phosphate dehydrogenase of
RT   Escherichia coli K-12.";
RL   J. Bacteriol. 170:2448-2456(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K.,
RA   Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
RA   Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
RA   Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
RA   Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
RA   Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-
RT   K12 genome corresponding to 50.0-68.8 min on the linkage map and
RT   analysis of its sequence features.";
RL   DNA Res. 4:91-113(1997).
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).
CC   -!- FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone.
CC       Uses fumarate or nitrate as electron acceptor.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC         dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC         ChEBI:CHEBI:132124; EC=1.1.5.3;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol
CC       kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate
CC       (anaerobic route): step 1/1.
CC   -!- SUBUNIT: Composed of a catalytic GlpA/B dimer and of membrane
CC       bound GlpC.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane
CC       protein. Note=Loosely bound to the cytoplasmic membrane often
CC       occurring in vesicles associated with fumarate reductase.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; M20938; AAA83864.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75301.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16060.1; -; Genomic_DNA.
DR   PIR; A32006; DEECNA.
DR   RefSeq; NP_416744.1; NC_000913.3.
DR   RefSeq; WP_000857257.1; NZ_LN832404.1.
DR   ProteinModelPortal; P0A9C0; -.
DR   SMR; P0A9C0; -.
DR   BioGrid; 4259614; 348.
DR   IntAct; P0A9C0; 4.
DR   STRING; 316385.ECDH10B_2400; -.
DR   jPOST; P0A9C0; -.
DR   PaxDb; P0A9C0; -.
DR   PRIDE; P0A9C0; -.
DR   EnsemblBacteria; AAC75301; AAC75301; b2241.
DR   EnsemblBacteria; BAA16060; BAA16060; BAA16060.
DR   GeneID; 946713; -.
DR   KEGG; ecj:JW2235; -.
DR   KEGG; eco:b2241; -.
DR   PATRIC; fig|1411691.4.peg.4498; -.
DR   EchoBASE; EB0386; -.
DR   EcoGene; EG10391; glpA.
DR   eggNOG; ENOG4107R5Y; Bacteria.
DR   eggNOG; COG0578; LUCA.
DR   HOGENOM; HOG000004814; -.
DR   InParanoid; P0A9C0; -.
DR   KO; K00111; -.
DR   PhylomeDB; P0A9C0; -.
DR   BioCyc; EcoCyc:ANGLYC3PDEHYDROGSUBUNITA-MONOMER; -.
DR   BioCyc; ECOL316407:JW2235-MONOMER; -.
DR   BioCyc; MetaCyc:ANGLYC3PDEHYDROGSUBUNITA-MONOMER; -.
DR   UniPathway; UPA00618; UER00673.
DR   PRO; PR:P0A9C0; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoCyc.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IDA:EcoCyc.
DR   GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IBA:GO_Central.
DR   GO; GO:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009061; P:anaerobic respiration; IEP:EcoCyc.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IDA:EcoCyc.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000447; G3P_DH_FAD-dep.
DR   InterPro; IPR017752; G3P_DH_GlpA_su.
DR   PANTHER; PTHR11985; PTHR11985; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF04324; Fer2_BFD; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR03377; glycerol3P_GlpA; 1.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
DR   PROSITE; PS00978; FAD_G3PDH_2; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Complete proteome;
KW   Direct protein sequencing; FAD; Flavoprotein; Membrane;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN         1    542       Anaerobic glycerol-3-phosphate
FT                                dehydrogenase subunit A.
FT                                /FTId=PRO_0000126093.
FT   NP_BIND      10     38       FAD. {ECO:0000255}.
FT   CONFLICT    329    329       V -> L (in Ref. 1; AAA83864).
FT                                {ECO:0000305}.
SQ   SEQUENCE   542 AA;  58958 MW;  E5C803F89E912E0E CRC64;
     MKTRDSQSSD VIIIGGGATG AGIARDCALR GLRVILVERH DIATGATGRN HGLLHSGARY
     AVTDAESARE CISENQILKR IARHCVEPTN GLFITLPEDD LSFQATFIRA CEEAGISAEA
     IDPQQARIIE PAVNPALIGA VKVPDGTVDP FRLTAANMLD AKEHGAVILT AHEVTGLIRE
     GATVCGVRVR NHLTGETQAL HAPVVVNAAG IWGQHIAEYA DLRIRMFPAK GSLLIMDHRI
     NQHVINRCRK PSDADILVPG DTISLIGTTS LRIDYNEIDD NRVTAEEVDI LLREGEKLAP
     VMAKTRILRA YSGVRPLVAS DDDPSGRNVS RGIVLLDHAE RDGLDGFITI TGGKLMTYRL
     MAEWATDAVC RKLGNTRPCT TADLALPGSQ EPAEVTLRKV ISLPAPLRGS AVYRHGDRTP
     AWLSEGRLHR SLVCECEAVT AGEVQYAVEN LNVNSLLDLR RRTRVGMGTC QGELCACRAA
     GLLQRFNVTT SAQSIEQLST FLNERWKGVQ PIAWGDALRE SEFTRWVYQG LCGLEKEQKD
     AL
//
DBGET integrated database retrieval system