ID A0A498KGR1_MALDO Unreviewed; 660 AA.
AC A0A498KGR1;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 10.
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=DVH24_005283 {ECO:0000313|EMBL:RXI07510.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXI07510.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXI07510.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXI07510.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-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:RXI07510.1}.
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DR EMBL; RDQH01000327; RXI07510.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498KGR1; -.
DR STRING; 3750.A0A498KGR1; -.
DR Proteomes; UP000290289; Chromosome 1.
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:UP000290289};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..660
FT /note="Glycerol-3-phosphate dehydrogenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019716833"
FT DOMAIN 76..444
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 466..600
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 660 AA; 71448 MW; 3758FA1EDCE54494 CRC64;
MATAIHLRRL GAAAVVATAA SGAFLLQPSL SASDRGAGSS SLGAVRQRIS DPNAVVPSRA
AQEAALIGAS AANPLDILVI GGGATGCGVA LDATTRGLRV GLVEREDFSS GTSSRSTKLI
HGGVRYLEKA VFNLDYGQLK LVFHALEERK QVIDNAPHLC HALPCMTPCF DWFEVVYYWM
GLKMYDLVAA LRLLHVSRYY SAQESVELFP TLARKGNNKS LKGTVVYYDG QMNDARLNVG
LACTAALAGA AVLNHAEVVD LLKDEASNRT IGARIRDNLS GKEFNTYAKV VVNAAGPFCD
SLRKMTDQDA KPMICPSSGV HIVLPDYYSP EGMGLIVPKT KDGRVVFMLP WLGRTIAGTT
DSNTPITLLP EPHEDEIQFI LDAICDYLNV KVRRTDVLSA WSGIRPLATD PSAKSTESIS
RDHVVCEDYP GLVTITGGKW TTYRGMAEDA VNAAIKSGKL TPENGCLTSK LQIVGGDGWD
PASFTVIAQQ YVRMKNSHGK VVPGVMDTAA AKHLSHAYGT LAERVAAIAQ NENLGKRLAH
GYPFLEAEVA YCARNEYCES AIDFIARRSR LAFLDTDAAS RALPRVIEIL ATEHNWDDSR
QKYELEKAKE FLKTFKSSKN AQFVHSFFTG TLTGGIFSGL NSGAKEYACH TQHMVIVTHL
//
