ID A0A2H3GK51_FUSOX Unreviewed; 682 AA.
AC A0A2H3GK51;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-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=AU210_013343 {ECO:0000313|EMBL:PCD26924.1};
OS Fusarium oxysporum f. sp. radicis-cucumerinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=327505 {ECO:0000313|EMBL:PCD26924.1, ECO:0000313|Proteomes:UP000219602};
RN [1] {ECO:0000313|EMBL:PCD26924.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD26924.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=27387256; DOI=10.1111/1462-2920.13445;
RA van Dam P., Fokkens L., Schmidt S.M., Linmans J.H., Kistler H.C., Ma L.J.,
RA Rep M.;
RT "Effector profiles distinguish formae speciales of Fusarium oxysporum.";
RL Environ. Microbiol. 18:4087-4102(2016).
RN [2] {ECO:0000313|EMBL:PCD26924.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD26924.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=28831051; DOI=10.1038/s41598-017-07995-y;
RA van Dam P., Fokkens L., Ayukawa Y., van der Gragt M., Ter Horst A.,
RA Brankovics B., Houterman P.M., Arie T., Rep M.;
RT "A mobile pathogenicity chromosome in Fusarium oxysporum for infection of
RT multiple cucurbit species.";
RL Sci. Rep. 7:9042-9042(2017).
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:PCD26924.1}.
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DR EMBL; MABQ02000009; PCD26924.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3GK51; -.
DR STRING; 327505.A0A2H3GK51; -.
DR OrthoDB; 989271at2759; -.
DR Proteomes; UP000219602; Chromosome 11.
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:UP000219602}.
FT DOMAIN 81..454
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 494..614
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 633..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 682 AA; 73841 MW; 8615C89F8404960C CRC64;
MQQRLRSLKR PLLLAAAATT TVTLGGAYYA SRNKTHVVDK PLVPLKRDEK NRIVPPTFNA
TKTRASQLAE LRRSGEDTEY DLLIIGGGAT GTGIAVDAIT RGLKVALVER DDFSSGTSSK
STKLVHGGVR YLEKAVWNLD YGQLQLVMEA LRERKTFLNI APHLSSSLPI LLPLQKWWEA
PYFWAGTKAY DLLAGSQGLE SSYYMSKNKA LEAFPLLRRE NMVGALVYYD GQHNDSRMNV
ALALTASHYG ATVLNHVEVT GLEKDANGKI MGAQVRDVLA SKNGDAAGAQ PFKVRAKGVV
NATGPFTDAI HQMDDPSRKP IVAPASGVHI MLPKEICPNG LGLLDAATSD GRVIFVLPWQ
GYTLAGTTDN PCEVEAAPVA QQQDVDFILK EVSKLLTPES VLSRKDVLAA WSGIRPLVKN
PNAKNTESLV RSHLITTSPS GLLTCAGGKW TTYREMAEDT VNEAIKLFDL KPQAVALPDI
SGAGASGFTT RGVCCTRNVP LIGAHGYSTS LASQLMEVYN IDADIADHLA HNYGDRAWTL
LSISPSLNTR LVSSLPFIEA EVSHGIRSEA ACTIPDIIAR RTRLSFLDSH KALEALPRVL
DIASTELQWS AARKEQEKAD AIKFLASMGL EQQTDAPVQA SQEEKMPVRS IEHSPRPTRV
GGLDVDLNGL GGTGSYSKSR DD
//
