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Database: UniProt
Entry: G8ZNZ4_TORDC
LinkDB: G8ZNZ4_TORDC
Original site: G8ZNZ4_TORDC 
ID   G8ZNZ4_TORDC            Unreviewed;       643 AA.
AC   G8ZNZ4;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   05-JUN-2019, entry version 32.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   Name=TDEL0B02090 {ECO:0000313|EMBL:CCE90338.1};
GN   ORFNames=TDEL_0B02090 {ECO:0000313|EMBL:CCE90338.1};
OS   Torulaspora delbrueckii (strain ATCC 10662 / CBS 1146 / NBRC 0425 /
OS   NCYC 2629 / NRRL Y-866) (Yeast) (Candida colliculosa).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Torulaspora.
OX   NCBI_TaxID=1076872 {ECO:0000313|Proteomes:UP000005627};
RN   [1] {ECO:0000313|EMBL:CCE90338.1, ECO:0000313|Proteomes:UP000005627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10662 / CBS 1146 / NBRC 0425 / NCYC 2629 / NRRL Y-866
RC   {ECO:0000313|Proteomes:UP000005627};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S.,
RA   Byrne K.P., Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type
RT   switching accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE616743; CCE90338.1; -; Genomic_DNA.
DR   RefSeq; XP_003679549.1; XM_003679501.1.
DR   STRING; 4950.XP_003679549.1; -.
DR   EnsemblFungi; CCE90338; CCE90338; TDEL_0B02090.
DR   GeneID; 11504259; -.
DR   KEGG; tdl:TDEL_0B02090; -.
DR   InParanoid; G8ZNZ4; -.
DR   KO; K00111; -.
DR   Proteomes; UP000005627; Chromosome 2.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
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   Gene3D; 1.10.8.870; -; 1.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR031656; DAO_C.
DR   InterPro; IPR038299; DAO_C_sf.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000447; G3P_DH_FAD-dep.
DR   PANTHER; PTHR11985; PTHR11985; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16901; DAO_C; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
DR   PROSITE; PS00978; FAD_G3PDH_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005627};
KW   Flavoprotein {ECO:0000256|RuleBase:RU361217};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU361217};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005627};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25    643       Glycerol-3-phosphate dehydrogenase.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003519506.
FT   DOMAIN       73    466       DAO. {ECO:0000259|Pfam:PF01266}.
FT   DOMAIN      487    627       DAO_C. {ECO:0000259|Pfam:PF16901}.
FT   REGION      294    315       Disordered. {ECO:0000256|MobiDB-lite:
FT                                G8ZNZ4}.
SQ   SEQUENCE   643 AA;  71027 MW;  BE3CBD876FB85743 CRC64;
     MFARAGRSLW PRAVALTAAA TVAGMGAVKY NDSVEQRRIA NDVALQSAVD TPNVKLPSRE
     DLLSKLSKTD QFDVLVIGGG ATGTGCAVDA ATRGLNVALV EMHDFASGTS SKSTKMAHGG
     VRYLEKAVFQ LSKAQLDLVI EALNERGHML NTAPHLCKIL PIMIPVYTYW QIPYFYVGCK
     MYDLFAGSQN LKNSYLLTKR QAADIAPMLD PTTLKAGLVY HDGSFNDSRM NTALAVTAIE
     NGATVLNYME VKQLIKDKET GKVQGALVTN RETGEQFTVK AKVTVNATGP YSDKLLQMDE
     NKDGKPDPTK PLPNATISTK VAVENPKMVV PSAGVHIILP SFYCPREMGL LDVKTSDGRV
     MFFLPWQGKV LAGTTDIPMK QVPQTPTAAE SDIQDILQEL QHYIKFPVKR EDVLSAWAGI
     RPLVIDPRKS QGNTGGSTQG LVRSHLCFTT DNGMVTIAGG KWTTYREMAE ETINEVVKVG
     KFNVKPCITR KLKLSGAENW NPNLAALLAQ KYHLSGAMSN HLSENYGTRA PLICEMFQED
     ERNQLPVTFG GRENVTVYGN VNFDSFRYPF TIGELNYSVD YEYTRTALDF LMRRTRFAFL
     DARQALDAVE GTVTVMGDKL NWDSTRRKHE IEKSKEFIRT FGV
//
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