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
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