ID W9IQD5_FUSOX Unreviewed; 519 AA.
AC W9IQD5;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Fumarate reductase {ECO:0000256|RuleBase:RU366062};
DE EC=1.3.1.6 {ECO:0000256|RuleBase:RU366062};
GN ORFNames=FOYG_04538 {ECO:0000313|EMBL:EWY95510.1};
OS Fusarium oxysporum NRRL 32931.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660029 {ECO:0000313|EMBL:EWY95510.1, ECO:0000313|Proteomes:UP000030753};
RN [1] {ECO:0000313|EMBL:EWY95510.1, ECO:0000313|Proteomes:UP000030753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Irreversibly catalyzes the reduction of fumarate to
CC succinate. {ECO:0000256|RuleBase:RU366062}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + succinate = fumarate + H(+) + NADH;
CC Xref=Rhea:RHEA:18281, ChEBI:CHEBI:15378, ChEBI:CHEBI:29806,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.6;
CC Evidence={ECO:0000256|RuleBase:RU366062};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU366062};
CC Note=Binds 1 FAD per monomer. {ECO:0000256|RuleBase:RU366062};
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000256|RuleBase:RU366062}.
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DR EMBL; JH717841; EWY95510.1; -; Genomic_DNA.
DR AlphaFoldDB; W9IQD5; -.
DR HOGENOM; CLU_011398_4_5_1; -.
DR OrthoDB; 1605658at2759; -.
DR Proteomes; UP000030753; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016156; F:fumarate reductase (NADH) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR010960; Flavocytochrome_c.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR NCBIfam; TIGR01813; flavo_cyto_c; 1.
DR PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR PANTHER; PTHR43400:SF1; FUMARATE REDUCTASE; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR PRINTS; PR00368; FADPNR.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU366062};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU366062};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU366062};
KW Reference proteome {ECO:0000313|Proteomes:UP000030753}.
FT DOMAIN 53..500
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 519 AA; 55083 MW; F46082E3D73D7057 CRC64;
MPRILRWTMS RPQILFLSCI GFAVALTAML YGNIIKTSTV TSVFSKTMST RPVVVVGSGL
AGLSASYEAL QHGAPSVHLL DRAPKPGGNS IKASSGINGA GTKFQRAAGV ESDTLFYSDS
VRSAGSRFHL TQPPVDREAL ITKLTTESAA AVNWLVDEIG VDLSVVAPLG GHSIARTHRG
AGKTPPGAAI IIALLNKLKE NGKFSITNLA EVKALLKEGN TVKGVEYELE GKRHNIEGSV
LFASGGFAGD ATGLLARYRP DLKGIPSTNE ERPGSHDILT AVGAELLDMD SVQIHPTGFV
DPATPNSMLK FLAAEMLRGE GGILLSPEGS RFVNEMDTRE HVSNAIMKLP TATDGDGVIK
QWDITILLDP GASAASANHI GFYEWKGLLK KVKVRDLKPA QIAALDKYAK AVAEGTDDEF
GRKQRGRWTL KAGEENRDED IYIGRVTPIT HFTMGGVAID QKARVLKKSE DKLVPIPGLF
AAGEITGGIH GDNRLGGSSL LECVVYGRTA GAEVVGSAQ
//
