OSM1_SCHPO
ID OSM1_SCHPO Reviewed; 513 AA.
AC O13755;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Fumarate reductase;
DE Short=FRDS;
DE EC=1.3.1.6;
DE AltName: Full=FAD-dependent oxidoreductase;
DE AltName: Full=NADH-dependent fumarate reductase;
GN Name=osm1; ORFNames=SPAC17A2.05;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Irreversibly catalyzes the reduction of fumarate to
CC succinate. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per monomer. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC Mitochondrion {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAB16560.1; -; Genomic_DNA.
DR PIR; T37806; T37806.
DR RefSeq; NP_594239.1; NM_001019662.2.
DR AlphaFoldDB; O13755; -.
DR SMR; O13755; -.
DR BioGRID; 278681; 2.
DR STRING; 4896.SPAC17A2.05.1; -.
DR iPTMnet; O13755; -.
DR MaxQB; O13755; -.
DR PaxDb; O13755; -.
DR PRIDE; O13755; -.
DR EnsemblFungi; SPAC17A2.05.1; SPAC17A2.05.1:pep; SPAC17A2.05.
DR GeneID; 2542206; -.
DR KEGG; spo:SPAC17A2.05; -.
DR PomBase; SPAC17A2.05; osm1.
DR VEuPathDB; FungiDB:SPAC17A2.05; -.
DR eggNOG; KOG2404; Eukaryota.
DR HOGENOM; CLU_011398_4_5_1; -.
DR InParanoid; O13755; -.
DR OMA; EDLWVVV; -.
DR PhylomeDB; O13755; -.
DR PRO; PR:O13755; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016156; F:fumarate reductase (NADH) activity; ISS:PomBase.
DR GO; GO:0006106; P:fumarate metabolic process; ISS:PomBase.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IC:PomBase.
DR Gene3D; 3.50.50.60; -; 1.
DR Gene3D; 3.90.700.10; -; 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 Pfam; PF00890; FAD_binding_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF56425; SSF56425; 1.
DR TIGRFAMs; TIGR01813; flavo_cyto_c; 1.
PE 3: Inferred from homology;
KW Cytoplasm; FAD; Flavoprotein; Mitochondrion; NAD; Nucleus; Oxidoreductase;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..513
FT /note="Fumarate reductase"
FT /id="PRO_0000316583"
FT ACT_SITE 288
FT /evidence="ECO:0000250"
FT ACT_SITE 311
FT /evidence="ECO:0000250"
FT BINDING 41..55
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 513 AA; 55484 MW; 9906AD63A570EC11 CRC64;
MRCLTIYTWT FRRLPFIPST NSASFFSTLR FNMSTANNTQ AIVIGGGLAG LSATNTILDL
GGNVLLLDKN TAFGGNSVKA ASGINAAPTQ LQFDQHVSDS VNTFYNDSIL SAKSKAKPEL
LRTLTSKSSS AVDWLSERFG LQMDQLSRLA GHSEPRTHRG THPDYPFKPL AFVLVDQTEK
FAASHPDRLQ IKKNARVTRL LTNPNHDKVF GVEYMDLSDK SNHTVYGPVV LATGGYAADY
SDDSLLKLYH PEALSLSTTN GPYCTGDGHK MVMSIGGSTV DLDLVQIHPT GFVDPKDPTA
LTKFLAAEAL RGSGAVLLTS QGRRFCDELG YRDYVTGEMM KLKSPVYLVL NSAAAEEVAN
FIKFYSFKGL MKKMKAEELC STLNCTKDEL ASTFSEYNRA AKGEIPDEFG RKYFGKTPLE
LTDTFTVGEV VPVLHYTMGG VQVDTQSRVL STNGNVIDGL FAAGEIVGGI HGENRLGGSS
LLACVVFGRL AGQGASSTML RRFIASSTST ASS
