ID N1RDB7_FUSC4 Unreviewed; 679 AA.
AC N1RDB7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=FOC4_g10005981 {ECO:0000313|EMBL:EMT62367.1};
OS Fusarium oxysporum f. sp. cubense (strain race 4) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=2502994 {ECO:0000313|EMBL:EMT62367.1, ECO:0000313|Proteomes:UP000016929};
RN [1] {ECO:0000313|Proteomes:UP000016929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RA Fang X., Huang J.;
RT "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000016929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RX PubMed=24743270;
RA Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA Fang X., Peng M., Huang J.;
RT "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL PLoS ONE 9:E95543-E95543(2014).
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; KB726995; EMT62367.1; -; Genomic_DNA.
DR AlphaFoldDB; N1RDB7; -.
DR STRING; 1229665.N1RDB7; -.
DR HOGENOM; CLU_015740_4_1_1; -.
DR Proteomes; UP000016929; 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:UP000016929}.
FT DOMAIN 86..457
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 500..627
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 679 AA; 75091 MW; 5ADD7404EAA2A3E9 CRC64;
MPAFAGAPRG LIRRFWLPGV VTTSAAVLIY SYRPRDFTGH TSPAVPPPTF GADGTFKLPR
FPRVKTREEQ LDQLRGSSRP QVQQYDILVI GGGATGAGVA LDAATRGLKV AVVERDDFSS
GTSSKSTKLV HGGVRYLEKA VWNLDYNQYL LVKEALKERK YFLQTAPHLS SWLPIMLPLD
KWWKAPYYWA GTKFYDFLAG SEGIEGSYFL TRSKALEAFP MLKPTDLVGA LVYYDGAHND
SRMNVSIAMT AALYGATVVN HAEVTGLIKN GDGNLCGAIV RDLVSVKDGR PAEVITVRAK
SVINCTGPFT DSVRKMDDPG CKEIVAPASG VHVILPGYFS PGKMGLIDPS TSDGRVIFFL
PWQGNTIAGT TDSPSTITPN PLPDEKSIEW ILSEISHYLS PEINVRRGDV LAAWSGIRPL
VKDPKAKNTE SLVRNHLIDI SASGLLTCAG GKWTTYRQMA EECVDFAIQE FRLEPRPVAD
APRVSGTDLI DDGAILDGKC QTHKVRLLGA HGFSPTLFIP IIQHFGVETE VAKHLTESYG
DRAWTVASLC KLTDKRFPAR GERISQLYPF VDGEIRYAIR HEYAQTAVDV LARRTRLAFL
NAQAALEALP KVIDIMAEEL KWSRQRKDLE WKESVAYLES MGLPKPMLTV TRKQVEQGKL
DFASSLEWQM YSRHDKPTD
//
