ID V5FKD3_BYSSN Unreviewed; 477 AA.
AC V5FKD3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Fumarate reductase {ECO:0000256|RuleBase:RU366062};
DE EC=1.3.1.6 {ECO:0000256|RuleBase:RU366062};
GN ORFNames=PVAR5_7041 {ECO:0000313|EMBL:GAD98349.1};
OS Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD98349.1, ECO:0000313|Proteomes:UP000018001};
RN [1] {ECO:0000313|Proteomes:UP000018001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA Oka T., Ekino K., Fukuda K., Nomura Y.;
RT "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL Genome Announc. 2:E0116213-E0116213(2014).
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}.
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:GAD98349.1}.
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DR EMBL; BAUL01000242; GAD98349.1; -; Genomic_DNA.
DR AlphaFoldDB; V5FKD3; -.
DR eggNOG; KOG2404; Eukaryota.
DR HOGENOM; CLU_011398_4_5_1; -.
DR InParanoid; V5FKD3; -.
DR OrthoDB; 1605658at2759; -.
DR Proteomes; UP000018001; 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 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:UP000018001}.
FT DOMAIN 13..451
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 477 AA; 50714 MW; 09607FFD014530C6 CRC64;
MTAPVPAIRE QCVIVVGSGL AGLAAASQLV ANNVPVRMLE TLAKPGGNSI KASSGINGAP
TRFQPGPDNR FYDDTIQSAG AAISQEDPDR LLRESLISVL TKSSADAVYW LADEKKVDLS
KVAQLGGHSR PRTHRGAGAN PPGRSIIGAL LSSLESNSRF HLHTNCKVTN IIREADEIKG
VGYRCEDGKT DTLLGPVVVT TGGFAGDANG MLAKYRPDLA GFPSTNEPRE GSQPLLTAVG
ARLLDMDRVQ VHPTGFVDTS SPSSPVKFLA AEALRGEGGI LLLPNGSRFV NETGTREYIT
NVIRNVASPT DTTSRQWDLD IVLDEGSAAA VGSSIDFYTW KDLLRKETVK DLGPEAISSL
QTYSDAASGK TKDPFGRQHF GHWTLKDVTP DSVVYVGKVT PVVHFTMGGV AINERSEVLD
KETNQPIRGL WAAGEVTGGI HGDNRLGGSS LLECVVFGRI AGEGAAEFYK ENYESEG
//
