FRDS_YEAST
ID FRDS_YEAST Reviewed; 470 AA.
AC P32614; D3DLK3;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Fumarate reductase 1;
DE Short=FRDS1;
DE EC=1.3.1.6;
DE AltName: Full=FAD-dependent oxidoreductase;
DE AltName: Full=NADH-dependent fumarate reductase;
DE AltName: Full=Soluble fumarate reductase, cytoplasmic isozyme;
GN Name=FRD1; Synonyms=FRDS, FRDS1; OrderedLocusNames=YEL047C;
GN ORFNames=SYGP-ORF35;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 89-106; 245-253;
RP 322-327 AND 409-423, COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=8946166; DOI=10.1093/dnares/3.4.263;
RA Enomoto K., Ohki R., Muratsubaki H.;
RT "Cloning and sequencing of the gene encoding the soluble fumarate reductase
RT from Saccharomyces cerevisiae.";
RL DNA Res. 3:263-267(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX DOI=10.1271/bbb1961.46.2909;
RA Muratsubaki H., Katsume T.;
RT "Purification and properties of fumarate reductase from baker's yeast.";
RL Agric. Biol. Chem. 40:2902-2917(1982).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=9587404; DOI=10.1006/abbi.1998.0583;
RA Muratsubaki H., Enomoto K.;
RT "One of the fumarate reductase isoenzymes from Saccharomyces cerevisiae is
RT encoded by the OSM1 gene.";
RL Arch. Biochem. Biophys. 352:175-181(1998).
RN [6]
RP FUNCTION.
RX PubMed=9711846; DOI=10.1111/j.1574-6968.1998.tb13134.x;
RA Arikawa Y., Enomoto K., Muratsubaki H., Okazaki M.;
RT "Soluble fumarate reductase isoenzymes from Saccharomyces cerevisiae are
RT required for anaerobic growth.";
RL FEMS Microbiol. Lett. 165:111-116(1998).
RN [7]
RP FUNCTION.
RX PubMed=12949191; DOI=10.1099/mic.0.26007-0;
RA Camarasa C., Grivet J.P., Dequin S.;
RT "Investigation by 13C-NMR and tricarboxylic acid (TCA) deletion mutant
RT analysis of pathways for succinate formation in Saccharomyces cerevisiae
RT during anaerobic fermentation.";
RL Microbiology 149:2669-2678(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP FUNCTION, AND INDUCTION.
RX PubMed=17345583; DOI=10.1002/yea.1467;
RA Camarasa C., Faucet V., Dequin S.;
RT "Role in anaerobiosis of the isoenzymes for Saccharomyces cerevisiae
RT fumarate reductase encoded by OSM1 and FRDS1.";
RL Yeast 24:391-401(2007).
CC -!- FUNCTION: Irreversibly catalyzes the reduction of fumarate to
CC succinate. Together with the second isozyme of soluble fumarate
CC reductase (OSM1), essential for anaerobic growth. Involved in
CC maintaining redox balance. Reduction of fumarate is the main source of
CC succinate during fermentation, and under anaerobic conditions, the
CC formation of succinate is strictly required for the reoxidation of
CC FADH(2). {ECO:0000269|PubMed:12949191, ECO:0000269|PubMed:17345583,
CC ECO:0000269|PubMed:9711846, ECO:0000269|Ref.4}.
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:0000269|Ref.4};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:8946166, ECO:0000269|Ref.4};
CC Note=Binds 1 FAD per monomer. {ECO:0000269|PubMed:8946166,
CC ECO:0000269|Ref.4};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 mM for fumarate {ECO:0000269|Ref.4};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8946166,
CC ECO:0000269|PubMed:9587404}.
CC -!- INDUCTION: During anaerobic growth. {ECO:0000269|PubMed:17345583}.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: Present with 7620 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000305}.
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DR EMBL; U18779; AAB64995.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07607.1; -; Genomic_DNA.
DR PIR; S30830; S30830.
DR RefSeq; NP_010867.3; NM_001178862.3.
DR AlphaFoldDB; P32614; -.
DR SMR; P32614; -.
DR BioGRID; 36683; 37.
DR DIP; DIP-5287N; -.
DR IntAct; P32614; 5.
DR MINT; P32614; -.
DR STRING; 4932.YEL047C; -.
DR iPTMnet; P32614; -.
DR MaxQB; P32614; -.
DR PaxDb; P32614; -.
DR PRIDE; P32614; -.
DR EnsemblFungi; YEL047C_mRNA; YEL047C; YEL047C.
DR GeneID; 856664; -.
DR KEGG; sce:YEL047C; -.
DR SGD; S000000773; FRD1.
DR VEuPathDB; FungiDB:YEL047C; -.
DR eggNOG; KOG2404; Eukaryota.
DR GeneTree; ENSGT00940000176615; -.
DR HOGENOM; CLU_011398_4_5_1; -.
DR InParanoid; P32614; -.
DR OMA; MAWAHGA; -.
DR BioCyc; MetaCyc:G3O-30165-MON; -.
DR BioCyc; YEAST:G3O-30165-MON; -.
DR PRO; PR:P32614; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P32614; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016156; F:fumarate reductase (NADH) activity; IDA:SGD.
DR GO; GO:0071454; P:cellular response to anoxia; IGI:SGD.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; NAD;
KW Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..470
FT /note="Fumarate reductase 1"
FT /id="PRO_0000158669"
FT ACT_SITE 249
FT /evidence="ECO:0000250"
FT ACT_SITE 272
FT /evidence="ECO:0000250"
FT BINDING 6..20
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT CONFLICT 285
FT /note="R -> K (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="V -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 470 AA; 50844 MW; 63C30B39252DC935 CRC64;
MSLSPVVVIG TGLAGLAAAN ELVNKYNIPV TILEKASSIG GNSIKASSGI NGACTETQRH
FHIEDSPRLF EDDTIKSAKG KGVQELMAKL ANDSPLAIEW LKNEFDLKLD LLAQLGGHSV
ARTHRSSGKL PPGFEIVSAL SNNLKKLAET KPELVKINLD SKVVDIHEKD GSISAVVYED
KNGEKHMVSA NDVVFCSGGF GFSKEMLKEY APELVNLPTT NGQQTTGDGQ RLLQKLGADL
IDMDQIQVHP TGFIDPNDRS SSWKFLAAES LRGLGGILLN PITGRRFVNE LTTRDVVTAA
IQKVCPQEDN RALLVMGEKM YTDLKNNLDF YMFKKLVQKL TLSQVVSEYN LPITVAQLCE
ELQTYSSFTT KADPLGRTVI LNEFGSDVTP ETVVFIGEVT PVVHFTMGGA RINVKAQVIG
KNDERLLKGL YAAGEVSGGV HGANRLGGSS LLECVVFGRT AAESIANDRK
