ID B2AMS7_PODAN Unreviewed; 527 AA.
AC B2AMS7;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Fumarate reductase {ECO:0000256|RuleBase:RU366062};
DE EC=1.3.1.6 {ECO:0000256|RuleBase:RU366062};
GN ORFNames=PODANS_5_5070 {ECO:0000313|EMBL:CAP65274.1};
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP65274.1};
RN [1] {ECO:0000313|EMBL:CAP65274.1, ECO:0000313|Proteomes:UP000001197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC {ECO:0000313|EMBL:CAP65274.1};
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2] {ECO:0000313|EMBL:CAP65274.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP65274.1};
RA Genoscope - CEA;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000001197}
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
RN [4] {ECO:0000313|EMBL:CDP29485.1}
RP NUCLEOTIDE SEQUENCE.
RA Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Submitted (APR-2015) 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; CU633871; CAP65274.1; -; Genomic_DNA.
DR EMBL; FO904940; CDP29485.1; -; Genomic_DNA.
DR RefSeq; XP_001905364.1; XM_001905329.1.
DR AlphaFoldDB; B2AMS7; -.
DR STRING; 515849.B2AMS7; -.
DR GeneID; 6189571; -.
DR KEGG; pan:PODANSg2389; -.
DR VEuPathDB; FungiDB:PODANS_5_5070; -.
DR eggNOG; KOG2404; Eukaryota.
DR HOGENOM; CLU_011398_4_5_1; -.
DR OrthoDB; 1605658at2759; -.
DR Proteomes; UP000001197; Chromosome 5.
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:UP000001197};
KW Signal {ECO:0000256|RuleBase:RU366062}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU366062"
FT CHAIN 21..527
FT /note="Fumarate reductase"
FT /evidence="ECO:0000256|RuleBase:RU366062"
FT /id="PRO_5007638971"
FT DOMAIN 48..508
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 527 AA; 56612 MW; 3ED5B612F8ED6392 CRC64;
MTRHHILSIL LLTILIPITA VLFHNYSAFS PVFRARFSQM ATTNKSPVIV VGAGLAGLSA
SYSAIQSGAS VRLLERAPKP GGNSIKASSG INGAPTRFQN VEKYGVDTSF WDDTTRSAGV
RLNSASVSPT VKRRREELIT VLTNRSASAI DFLTDLGVDL SVVAQLGGHS LPRTHRGAGK
TPPGASIVTT LLTKLKEQGP DRFQLVTDSE VTRLLTDSNA PKGTVKVTGV EYKNRQDGST
RLLHGPVVFT TGGFAGDTHG LLAKYRPDLD GLPSTNDPRP GTHTILSDVG AKLVDMDAVQ
IHPTGFIDPA NPASPLKFLA AEMLRGEGGI LLHNGKRVIN ELQTREKVSN ALMALPAKNE
DSLRQWDVQL LLDPGATEAA AGHVGFYLWK GLLQKKKIAE LDETTRQTLK EYAAVVRGEK
EDELGRKAFG NWRLTEEDVD EGEEEVCVGR VTPITHFTMG GAVFNTKAQI LTAELGEEQE
GKEIEGLWGA GEITGGLHGD NRLGGSSLLE CVVFGRVAGE EAAKYRV
//
