ID A0A137Q6T4_9AGAR Unreviewed; 790 AA.
AC A0A137Q6T4;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=AN958_02048 {ECO:0000313|EMBL:KXN82910.1};
OS Leucoagaricus sp. SymC.cos.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN82910.1, ECO:0000313|Proteomes:UP000070249};
RN [1] {ECO:0000313|EMBL:KXN82910.1, ECO:0000313|Proteomes:UP000070249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SymC.cos {ECO:0000313|EMBL:KXN82910.1,
RC ECO:0000313|Proteomes:UP000070249};
RA Hu H.;
RT "Leucoagaricus sp. SymC.cos WGS genome.";
RL Submitted (JAN-2016) 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}.
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DR EMBL; KQ962894; KXN82910.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137Q6T4; -.
DR STRING; 1714833.A0A137Q6T4; -.
DR OrthoDB; 989271at2759; -.
DR Proteomes; UP000070249; 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:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
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:UP000070249}.
FT DOMAIN 75..440
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 464..590
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 790 AA; 87060 MW; A28FDE468DFF005F CRC64;
MPLLRRLFSR RTLAYATGST MLATGGFYWY LNSGPAYPSS TKETRRPPPP WTPPSRAEML
AELRKSGERP EDEFDLLIVG GGATGAGVAV DAASRGLKVA LVERDDFAAG TSSKSTKLVH
GGVRYLQKAV FELDYDQYKL VREALHERRI FLQTAPYLSN MLPIMLPVYK YWQVPYYLAG
CKLYDILAGK ENMETSYVMS KGKALETFPM LKSDGLVGAV VYYDGQHNDS RMNIALIMSA
VKHGAAVANY CEVTKLHKND SGKLSGASVR DNLTGKEWSV RAKGIINATG PFADTLLTLD
NSSHQPIVQP SSGIHITLPN YYSPRKMGLL DPATSDGRVI FFLPWQGNTI AGTTDSPARV
SRNPSASEED IRWVLEEVRS YLSPDIKVRR GDVLSAWSGL RPLVRNPGAS STEGLVRSHM
IHVSESGLLT IAGGKWTTYR AMAEETVDEA VKVFGLEKKV KSGCVTDRLR LVGSDGWSRN
MFIGLIQTYG LDSDVAKHLS ENYGDRAWTV CALAEPTGES WPLHGKRLVS QYPFIEAEIR
YALKHEYALS AIDILARRTR LSFLNARAAL DALPRVIDIM SVELNWSRSE RNKQIRDAVD
FLVGSMSLDE GYVSGDVVRR VREHLQPRGW IERAEMSWWD ICGLVSRSFG KVGRSVGATA
VGVGERVRVL GRARFEVGEI GILKFFFDKH ATLVASHSGS GEDKGKINTT TILDVLKEVA
GYDAITKKEL QYVLEEAGFS ARDALDWDEF LEVCGGLREV SVSPADINGS GALKAKQRRV
IPVEKSGGGV
//
