ID GLPA_ECO57 Reviewed; 542 AA.
AC P0A9C1; P13032; P78238;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 127.
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=Z3499, ECs3126;
OS Escherichia coli O157:H7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses
CC fumarate or nitrate as electron acceptor (By similarity).
CC {ECO:0000250}.
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; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Note=Loosely bound to the cytoplasmic
CC membrane often occurring in vesicles associated with fumarate
CC reductase. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; AE005174; AAG57372.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36549.1; -; Genomic_DNA.
DR PIR; F91019; F91019.
DR RefSeq; NP_311153.1; NC_002695.1.
DR RefSeq; WP_000857257.1; NZ_VOAI01000001.1.
DR AlphaFoldDB; P0A9C1; -.
DR SMR; P0A9C1; -.
DR STRING; 155864.Z3499; -.
DR GeneID; 75205706; -.
DR GeneID; 916834; -.
DR KEGG; ece:Z3499; -.
DR KEGG; ecs:ECs_3126; -.
DR PATRIC; fig|386585.9.peg.3260; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_0_1_6; -.
DR OMA; GVMTIMN; -.
DR UniPathway; UPA00618; UER00673.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR CDD; cd19946; GlpA-like_Fer2_BFD-like; 1.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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 NCBIfam; TIGR03377; glycerol3P_GlpA; 1.
DR PANTHER; PTHR11985:SF36; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT A; 1.
DR PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF04324; Fer2_BFD; 1.
DR PRINTS; PR01001; FADG3PDH.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00977; FAD_G3PDH_1; 1.
DR PROSITE; PS00978; FAD_G3PDH_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; FAD; Flavoprotein; Membrane;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..542
FT /note="Anaerobic glycerol-3-phosphate dehydrogenase subunit
FT A"
FT /id="PRO_0000126094"
FT BINDING 10..38
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
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
//
