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   03-AUG-2022, entry version 129.
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., Itoh T.,
RA   Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA   Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA   Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA   Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT   genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT   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., Mau B.,
RA   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 MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
CC   -!- FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses
CC       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, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, 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 kinase
CC       pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic
CC       route): step 1/1.
CC   -!- SUBUNIT: Composed of a catalytic GlpA/B dimer and of membrane bound
CC       GlpC.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein.
CC       Note=Loosely bound to the cytoplasmic membrane often occurring in
CC       vesicles associated with fumarate reductase.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
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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   AlphaFoldDB; P0A9C0; -.
DR   SMR; P0A9C0; -.
DR   BioGRID; 4259614; 348.
DR   ComplexPortal; CPX-4841; Anaerobic glycerol-3-phosphate dehydrogenase complex.
DR   IntAct; P0A9C0; 4.
DR   STRING; 511145.b2241; -.
DR   jPOST; P0A9C0; -.
DR   PaxDb; P0A9C0; -.
DR   PRIDE; P0A9C0; -.
DR   EnsemblBacteria; AAC75301; AAC75301; b2241.
DR   EnsemblBacteria; BAA16060; BAA16060; BAA16060.
DR   GeneID; 66673870; -.
DR   GeneID; 946713; -.
DR   KEGG; ecj:JW2235; -.
DR   KEGG; eco:b2241; -.
DR   PATRIC; fig|1411691.4.peg.4498; -.
DR   EchoBASE; EB0386; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_0_1_6; -.
DR   InParanoid; P0A9C0; -.
DR   OMA; GVMTIMN; -.
DR   PhylomeDB; P0A9C0; -.
DR   BioCyc; EcoCyc:ANGLYC3PDEHYDROGSUBUNITA-MON; -.
DR   BioCyc; MetaCyc:ANGLYC3PDEHYDROGSUBUNITA-MON; -.
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; IC:ComplexPortal.
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: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; 1.10.10.1100; -; 1.
DR   Gene3D; 3.50.50.60; -; 3.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
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; Direct protein sequencing; FAD;
KW   Flavoprotein; Membrane; Oxidoreductase; Reference proteome.
FT   CHAIN           1..542
FT                   /note="Anaerobic glycerol-3-phosphate dehydrogenase subunit
FT                   A"
FT                   /id="PRO_0000126093"
FT   BINDING         10..38
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        329
FT                   /note="V -> L (in Ref. 1; AAA83864)"
FT                   /evidence="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