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Database: UniProt
Entry: D7NDV2_9BACT
LinkDB: D7NDV2_9BACT
Original site: D7NDV2_9BACT 
ID   D7NDV2_9BACT            Unreviewed;       540 AA.
AC   D7NDV2;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   ORFNames=HMPREF0665_01726 {ECO:0000313|EMBL:EFI48099.1};
OS   Segatella oris C735.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Segatella.
OX   NCBI_TaxID=563008 {ECO:0000313|EMBL:EFI48099.1, ECO:0000313|Proteomes:UP000003805};
RN   [1] {ECO:0000313|EMBL:EFI48099.1, ECO:0000313|Proteomes:UP000003805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C735 {ECO:0000313|EMBL:EFI48099.1,
RC   ECO:0000313|Proteomes:UP000003805};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA   Sibley C.D., Field T.R., Grinwis M., Eshaghurshan C.S., Surette M.G.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Prevotella oris strain C735.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|RuleBase:RU361217};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU361217};
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330,
CC       ECO:0000256|RuleBase:RU361217}.
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DR   EMBL; GL349569; EFI48099.1; -; Genomic_DNA.
DR   RefSeq; WP_004378013.1; NZ_GL349569.1.
DR   AlphaFoldDB; D7NDV2; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_0_1_10; -.
DR   Proteomes; UP000003805; Unassembled WGS sequence.
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:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) 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   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; 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   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
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   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU361217};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361217};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003805}.
FT   DOMAIN          10..359
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   540 AA;  58767 MW;  12E064FE37E84BBE CRC64;
     MNKEQHTTYD VIVIGGGITG AGVARDCAMR GLKVLLVEKY DLTNGATGRN HGLLHSGARY
     AVTDRESATE CIQENMTLRK IARHCVEETD GLFITLPEDD ILYQQTFVDA CRNAGIRADI
     IAPKEAIRLE PAVNPTLIGA VRVPDASIDP FRLTAANVLD ARLHGATVLT YHEVTRLIIN
     NGRVEGVVMR DNITGEMREA HAQLTINAAG IWGHLIAEMA DVPLNMFPAK GSLLIFGHRV
     NQMVINRCRK PANADILVPD DAVCVIGTTS DRVSYDVIDH LKVTPEEVDI LISEGEKLAP
     ALATTRILRA YAGVRPLVAA DNDPSGRNIS RGIVLLDHEK RDGLGGFITI TGGKMMTYRL
     MAELATDLAC KKLGVNKACE TAEKPLPGSE EKCSKKGLST ERLAEEGRHG TLASLIPDDA
     IMDKALVCEC EEVSVGEMKY AVDKLHVKNL INMRRRTRVS MGTCQGTLCA CRAACVLCNL
     TQTDAKKSQA DLASVMAERW KGMRPVAWGD TLKESQLMSM VYEGLCGLNQ RTGKGKEIAR
//
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