ID A0A2P7YZP0_9ASCO Unreviewed; 649 AA.
AC A0A2P7YZP0;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|ARBA:ARBA00013029, ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|ARBA:ARBA00013029, ECO:0000256|RuleBase:RU361217};
GN ORFNames=C7M61_001106 {ECO:0000313|EMBL:PSK41424.1};
OS [Candida] pseudohaemulonii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=418784 {ECO:0000313|EMBL:PSK41424.1, ECO:0000313|Proteomes:UP000241107};
RN [1] {ECO:0000313|EMBL:PSK41424.1, ECO:0000313|Proteomes:UP000241107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B12108 {ECO:0000313|EMBL:PSK41424.1,
RC ECO:0000313|Proteomes:UP000241107};
RA Munoz J.F., Gade L.G., Chow N.A., Litvintseva A.P., Loparev V.N.,
RA Cuomo C.A.;
RT "Candida pseudohaemulonii genome assembly and annotation.";
RL Submitted (MAR-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PSK41424.1}.
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DR EMBL; PYFQ01000001; PSK41424.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P7YZP0; -.
DR STRING; 418784.A0A2P7YZP0; -.
DR EnsemblFungi; C7M61_001106_t1; PSK41424.1; C7M61_001106.
DR VEuPathDB; FungiDB:C7M61_001106; -.
DR OrthoDB; 989271at2759; -.
DR Proteomes; UP000241107; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
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 Gene3D; 1.10.8.870; Alpha-glycerophosphate oxidase, cap domain; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11985:SF15; GLYCEROL-3-PHOSPHATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16901; DAO_C; 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:UP000241107}.
FT DOMAIN 69..448
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 473..619
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 649 AA; 72106 MW; D14C8183FA90F2D6 CRC64;
MSRFFKSTFF KTAAASASVV GAGVVYLDFV RSPNPSNFKN SYEPLRKKLD VPPSREELLN
NVKKTDKFDV LIVGGGATGT GTAVDAASRG LNVCLLERSD FASGTSSKST KMAHGGVRYL
EKAIFQLSKD QLDLVIEALN ERGNMLRTAP HLCSVLPIMI PVYKWWQVPY FFIGCKMYDW
FAGHQNLRSS TVFSAETFGA IAPMIDTANI KAACVYHDGT FNDARFNATL AVTAVDHGAT
VLNYMEVKQL IKEDGKLVGA LAVDKETGEE YRIKATATVN ATGPFADKLL EMDEDPQGLP
PKQEQAPRMV VPSSGVHIVL PEYYGPTSMG LLDPSTSDGR VMFFLPWQGK VLAGTTDTPL
KKVPNNPVPT EEEITDILGE LQKYIVFPVN REDVLSAWSG IRPLVQDPAK IPKGKDANSG
TQGLVRSYLI TISESGLLTI SGGKWTTYRE MAQETVDTLV KKYDFGGKNL KSCQTNKILL
AGGEDYSKNY SARLIHEYKI PLKLAKHLSH NYGSRAALIL ELYQQNDYNK LPITLAATHE
YIPNETKNTD GTILSYQSFD EPFTIAELKY SLQYEYIRHP LDFLARRTRL AFLNAREALS
AVDGVVEIMR NEFKWDDETT KRLSDETKEY ISLMGVSSQK FNVTDFVVQ
//
