(data stored in ACNUC9543 zone)
SWISSPROT: A0A0E1NST2_YERPA
ID A0A0E1NST2_YERPA Unreviewed; 551 AA.
AC A0A0E1NST2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 08-MAY-2019, entry version 24.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
DE Flags: Precursor;
GN OrderedLocusNames=YPA_0196 {ECO:0000313|EMBL:ABG12165.1};
OS Yersinia pestis bv. Antiqua (strain Antiqua).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12165.1, ECO:0000313|Proteomes:UP000001971};
RN [1] {ECO:0000313|EMBL:ABG12165.1, ECO:0000313|Proteomes:UP000001971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Antiqua {ECO:0000313|EMBL:ABG12165.1,
RC ECO:0000313|Proteomes:UP000001971};
RX PubMed=16740952; DOI=10.1128/JB.00124-06;
RA Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and
RT Nepal516: evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(2006).
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 Evidence={ECO:0000256|RuleBase:RU361217};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU361217};
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|RuleBase:RU361217}.
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DR EMBL; CP000308; ABG12165.1; -; Genomic_DNA.
DR RefSeq; WP_002211491.1; NZ_CP009906.1.
DR EnsemblBacteria; ABG12165; ABG12165; YPA_0196.
DR EnsemblBacteria; AJJ79926; AJJ79926; CH58_3041.
DR KEGG; ypa:YPA_0196; -.
DR PATRIC; fig|360102.15.peg.3193; -.
DR KO; K00111; -.
DR OMA; IRSFWGV; -.
DR Proteomes; UP000001971; Chromosome.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046174; P:polyol catabolic process; IEA:InterPro.
DR Gene3D; 1.10.10.1100; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
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 3: Inferred from homology;
DR PRODOM; A0A0E1NST2.
DR SWISS-2DPAGE; A0A0E1NST2.
KW Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW Flavoprotein {ECO:0000256|RuleBase:RU361217};
KW Oxidoreductase {ECO:0000256|RuleBase:RU361217}.
SQ SEQUENCE 551 AA; 60153 MW; 2E4A319DDEED1C8E CRC64;
MTNSSPYLET DVIIIGGGAT GAGIARDCAR RGLACTLLER HDIATGATGR NHGLLHSGAR
YAVTDGESAR ECIEENRILK RIARHCIEQT DGLFITLPED SLAYQLQFIA RCRDAGIEAE
AIDPAQALRL EPAVNPALIA AVRVPDGTVD PFRLTAANML DAREHGANIL TYHEVIGLLR
QGSRINGVCV FDHKNQRKYD IHAQIVVNAA GIWGQHIAEY ADLRIRMFPA KGALLILGHR
INNMVINRCR KPADADILVP GDTISLIGTT STHINYDQID NMVVTAQEVD TLIREGAKLS
PQLAQTRILR AYAGVRPLVA SDDDPSGRNV SRGIVLLDHA SRDGVEGFIT ITGGKLMTYR
LMAEWATDKV CEKLGISAAC TTAQVPLPGS RQSAEQTLSK VISLPASIRG SAVYRHGDRA
TQLLVGNRLD NSLVCECEAV TAGEVRYAVE SLSVNNLLDL RRRTRVGMGT CQGELCACRA
AGLLSRFKVT TPQQSREQLT QFLNERWKGV RPIAWGDALR ESEFTQWVYQ GLCGLDEIPA
TVNAREKHDE I
//
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