ID D7TM57_VITVI Unreviewed; 644 AA.
AC D7TM57;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
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 OrderedLocusNames=VIT_13s0019g04730 {ECO:0000313|EMBL:CBI31424.3};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CBI31424.3, ECO:0000313|Proteomes:UP000009183};
RN [1] {ECO:0000313|Proteomes:UP000009183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX PubMed=17721507; DOI=10.1038/nature06148;
RG The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
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; FN595998; CBI31424.3; -; Genomic_DNA.
DR AlphaFoldDB; D7TM57; -.
DR STRING; 29760.D7TM57; -.
DR PaxDb; 29760-VIT_13s0019g04730-t01; -.
DR EnsemblPlants; Vitvi13g00654_t001; Vitvi13g00654_P001; Vitvi13g00654.
DR Gramene; Vitvi13g00654_t001; Vitvi13g00654_P001; Vitvi13g00654.
DR eggNOG; KOG0042; Eukaryota.
DR HOGENOM; CLU_015740_4_3_1; -.
DR InParanoid; D7TM57; -.
DR OMA; PHIVKPM; -.
DR Proteomes; UP000009183; Chromosome 13.
DR ExpressionAtlas; D7TM57; baseline and differential.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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:UP000009183}.
FT DOMAIN 75..443
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 465..601
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 644 AA; 70663 MW; 4F48B7A2768CBBFF CRC64;
MATTSTRLRR LGTVAAAVAL SAGVTLRDPP ISSSDRGGPS LDAVRRKIAD SNGVVPSRAV
QESALIGSSA VNPLDILVVG GGATGCGVAL DAATRGLRVG LVEREDFSSG TSSRSTKLLH
GGVRYLEKAV FNLDYGQLKL VFHALEERKQ VIENAPHLCQ ALPCMTPCFD WFEVVYYWMG
LKLYDLVAGS RLLHLSRYYS AQESVELFPT LARNGKDRSL RGTVVYYDGQ MNDSRLNVAL
ACTAALAGAA VLNHAEVVSL LMDEVSNQII GARIRDNLSG KEFDTYAKVV VNAAGPFCDS
VRKMADKESQ PMICPSSGVH IVLPDYYSPE GMGLIVPKTK DGRVVFMLPW LGRTVAGTTD
SNTSITMLPE PHEDEIQFIL DAISDYLNVK VRRTDVLSAW SGIRPLAVDP KAKSTESISR
DHVVCEDHPG LVTITGGKWT TYRSMAEDAV DAAIKSGKLS PTNECLTNNL HLSGSEDWDP
ASFTVLAQQY VRMKRSHSGK VVPGVMDTAA AKHLSHAYGT MADRVAAIAQ DEHLGKRLAH
GYPFLEAEVA YCARNEYCES AVDFIARRSR LAFLDTDAAS RALPRIIGIL ATEHNWDRTR
KKKELQKAKE FLETFKSSRN AQFYDGKHKY WIFWELDLFN SHNQ
//
