ID A0A439DER5_9PEZI Unreviewed; 680 AA.
AC A0A439DER5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
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=EKO27_g2190 {ECO:0000313|EMBL:RWA12900.1};
OS Xylaria grammica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Xylaria.
OX NCBI_TaxID=363999 {ECO:0000313|EMBL:RWA12900.1, ECO:0000313|Proteomes:UP000286045};
RN [1] {ECO:0000313|EMBL:RWA12900.1, ECO:0000313|Proteomes:UP000286045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IHI A82 {ECO:0000313|EMBL:RWA12900.1,
RC ECO:0000313|Proteomes:UP000286045};
RA Buettner E., Kellner H.;
RT "Draft genome sequence of Xylaria grammica IHI A82.";
RL Submitted (DEC-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:RWA12900.1}.
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DR EMBL; RYZI01000039; RWA12900.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A439DER5; -.
DR STRING; 363999.A0A439DER5; -.
DR Proteomes; UP000286045; 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:UP000286045}.
FT DOMAIN 85..456
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 499..625
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 680 AA; 75375 MW; 64D4EC09503FA6E6 CRC64;
MTRFQRGTRL LRRLALPTSV AAVGGGLLLY SYRPLNIPGS EGPAVPPPLY GADGTFRLPR
FPKVKSRDEQ LAELKKSRSQ EDEYDILVIG GGATGAGVAL DAVTRGLKVA MVERDDFSSG
TSSKSTKLVH GGVRYLEKAV WNLDYAQYQL VREALKERKY FLQTAPHLSS WLPIMLPLDK
WWKAPYYWAG TKFYDFLAGS EGIESSYFLT RSKALDAFPM LKPTDLVGAL VYYDGAHNDS
RMNVSLAMTA ALYGATVVNH AEVTGLMKND NGKLCGATIK DRVPERGGRT TDDITVRAKC
IINCTGPFTD SIRKLDDQKC KEIVAPASGV HVILPGYYSP AKMGLIDPST SDGRVIFFLP
WQGNTIAGTT DESATITQNP LPDEKSIQWI LNEVSHYLAP EIQVRRGDVL AAWSGLRPLV
KDPKASNTES LVRNHLVDIS DSGLVTCAGG KWTTYRQMAE ECVDAAVKEF KLPTKPFPNA
PRVSGTEAID DGAILDGSCQ THNVRLIGAH GFSKTLFINL IQHFGVETEV AKHLTESYGD
RAWTVAALCK PTELRFPARG ERISQLYPFV DGEIRYAISH EYAQTAVDIL ARRTRLAFLN
AQAALECLPR IIDIMSQELH WDKTRQDREW KDTVSFLESM GLPKPMLSAT RADVEKGKLD
FSSSLEYKMF SRHDKPLLEE
//
