OSM1_YEAST
ID OSM1_YEAST Reviewed; 501 AA.
AC P21375; D6VWM2;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Fumarate reductase 2;
DE Short=FRDS2;
DE EC=1.3.1.6;
DE AltName: Full=NADH-dependent fumarate reductase;
DE AltName: Full=Osmotic sensitivity protein 1;
DE AltName: Full=Soluble fumarate reductase, mitochondrial isozyme;
DE Flags: Precursor;
GN Name=OSM1; OrderedLocusNames=YJR051W; ORFNames=J1659;
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 PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2158927; DOI=10.1016/0378-1119(90)90297-5;
RA Melnick L., Sherman F.;
RT "Nucleotide sequence of the COR region: a cluster of six genes in the yeast
RT Saccharomyces cerevisiae.";
RL Gene 87:157-166(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7975898; DOI=10.1002/yea.320100611;
RA Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
RT "Revised nucleotide sequence of the COR region of yeast Saccharomyces
RT cerevisiae chromosome X.";
RL Yeast 10:811-818(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
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 [5]
RP PROTEIN SEQUENCE OF 33-52 AND 487-501, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, AND 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 DISRUPTION PHENOTYPE.
RX PubMed=211068; DOI=10.1093/genetics/89.4.653;
RA Singh A., Sherman F.;
RT "Deletions of the iso-1-cytochrome c and adjacent genes of yeast: discovery
RT of the OSM1 gene controlling osmotic sensitivity.";
RL Genetics 89:653-665(1978).
RN [7]
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 [8]
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 [9]
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 [10]
RP FUNCTION.
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).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Irreversibly catalyzes the reduction of fumarate to
CC succinate. Together with the second isozyme of soluble fumarate
CC reductase (FRD1), essential for anaerobic growth. Involved in
CC maintaining redox balance during oxygen deficiency conditions.
CC Reduction of fumarate is the main source of succinate during
CC fermentation, and under anaerobic conditions, the formation of
CC succinate is strictly required for the reoxidation of FADH(2).
CC {ECO:0000269|PubMed:12949191, ECO:0000269|PubMed:17345583,
CC ECO:0000269|PubMed:9587404, ECO:0000269|PubMed:9711846}.
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|PubMed:9587404};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:9587404};
CC Note=Binds 1 FAD per monomer. {ECO:0000269|PubMed:9587404};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9587404}.
CC -!- DISRUPTION PHENOTYPE: Causes increased sensitivity to hypertonic growth
CC medium. {ECO:0000269|PubMed:211068}.
CC -!- MISCELLANEOUS: Present with 432 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB59346.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M37696; AAB59346.1; ALT_FRAME; Genomic_DNA.
DR EMBL; L26347; AAA62859.1; -; Genomic_DNA.
DR EMBL; L36344; AAA88754.1; -; Genomic_DNA.
DR EMBL; Z49551; CAA89579.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08838.1; -; Genomic_DNA.
DR PIR; S46591; S46591.
DR RefSeq; NP_012585.1; NM_001181709.1.
DR PDB; 5GLG; X-ray; 1.80 A; A=32-501.
DR PDB; 5ZYN; X-ray; 1.75 A; B=32-501.
DR PDB; 6KU6; X-ray; 2.01 A; B/H=32-501.
DR PDBsum; 5GLG; -.
DR PDBsum; 5ZYN; -.
DR PDBsum; 6KU6; -.
DR AlphaFoldDB; P21375; -.
DR SMR; P21375; -.
DR BioGRID; 33804; 81.
DR DIP; DIP-5426N; -.
DR IntAct; P21375; 2.
DR MINT; P21375; -.
DR STRING; 4932.YJR051W; -.
DR iPTMnet; P21375; -.
DR MaxQB; P21375; -.
DR PaxDb; P21375; -.
DR PRIDE; P21375; -.
DR EnsemblFungi; YJR051W_mRNA; YJR051W; YJR051W.
DR GeneID; 853510; -.
DR KEGG; sce:YJR051W; -.
DR SGD; S000003812; OSM1.
DR VEuPathDB; FungiDB:YJR051W; -.
DR eggNOG; KOG2404; Eukaryota.
DR GeneTree; ENSGT00940000176615; -.
DR HOGENOM; CLU_011398_4_5_1; -.
DR InParanoid; P21375; -.
DR OMA; RLMGNAL; -.
DR BioCyc; MetaCyc:YJR051W-MON; -.
DR BioCyc; YEAST:YJR051W-MON; -.
DR PRO; PR:P21375; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P21375; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016156; F:fumarate reductase (NADH) activity; IDA:SGD.
DR GO; GO:0046443; P:FAD metabolic process; IMP:SGD.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; IMP: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 3D-structure; Direct protein sequencing; FAD; Flavoprotein; Mitochondrion;
KW NAD; Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:9587404"
FT CHAIN 33..501
FT /note="Fumarate reductase 2"
FT /id="PRO_0000158668"
FT ACT_SITE 281
FT /evidence="ECO:0000250"
FT ACT_SITE 304
FT /evidence="ECO:0000250"
FT BINDING 37..51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT CONFLICT 106..107
FT /note="LH -> FD (in Ref. 1; AAB59346)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="A -> AR (in Ref. 1; AAB59346)"
FT /evidence="ECO:0000305"
FT CONFLICT 191..192
FT /note="Missing (in Ref. 1; AAB59346)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="G -> S (in Ref. 1; AAB59346)"
FT /evidence="ECO:0000305"
FT CONFLICT 456..457
FT /note="SV -> TL (in Ref. 1; AAB59346)"
FT /evidence="ECO:0000305"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:5ZYN"
FT HELIX 44..57
FT /evidence="ECO:0007829|PDB:5ZYN"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:5ZYN"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:5ZYN"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:5ZYN"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:5ZYN"
FT HELIX 98..109
FT /evidence="ECO:0007829|PDB:5ZYN"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:5ZYN"
FT HELIX 125..136
FT /evidence="ECO:0007829|PDB:5ZYN"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:5ZYN"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:5ZYN"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:5ZYN"
FT HELIX 163..181
FT /evidence="ECO:0007829|PDB:5ZYN"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:5ZYN"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:5ZYN"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:5ZYN"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:5ZYN"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:5ZYN"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:5ZYN"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:5ZYN"
FT HELIX 236..242
FT /evidence="ECO:0007829|PDB:5ZYN"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:5ZYN"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:5ZYN"
FT HELIX 260..267
FT /evidence="ECO:0007829|PDB:5ZYN"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:5ZYN"
FT STRAND 278..285
FT /evidence="ECO:0007829|PDB:5ZYN"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:5ZYN"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:5ZYN"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:5ZYN"
FT HELIX 326..336
FT /evidence="ECO:0007829|PDB:5ZYN"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:5GLG"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:5ZYN"
FT HELIX 350..354
FT /evidence="ECO:0007829|PDB:5ZYN"
FT HELIX 357..365
FT /evidence="ECO:0007829|PDB:5ZYN"
FT STRAND 368..373
FT /evidence="ECO:0007829|PDB:5ZYN"
FT HELIX 374..380
FT /evidence="ECO:0007829|PDB:5ZYN"
FT HELIX 387..398
FT /evidence="ECO:0007829|PDB:5ZYN"
FT STRAND 424..437
FT /evidence="ECO:0007829|PDB:5ZYN"
FT STRAND 440..443
FT /evidence="ECO:0007829|PDB:5ZYN"
FT STRAND 447..451
FT /evidence="ECO:0007829|PDB:5ZYN"
FT STRAND 454..458
FT /evidence="ECO:0007829|PDB:5ZYN"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:5ZYN"
FT STRAND 469..473
FT /evidence="ECO:0007829|PDB:5ZYN"
FT HELIX 481..500
FT /evidence="ECO:0007829|PDB:5ZYN"
SQ SEQUENCE 501 AA; 55065 MW; DDBF803BC342A5F9 CRC64;
MIRSVRRVFI YVSIFVLIIV LKRTLSGTDQ TSMKQPVVVI GSGLAGLTTS NRLISKYRIP
VVLLDKAASI GGNSIKASSG INGAHTDTQQ NLKVMDTPEL FLKDTLHSAK GRGVPSLMDK
LTKESKSAIR WLQTEFDLKL DLLAQLGGHS VPRTHRSSGK LPPGFEIVQA LSKKLKDISS
KDSNLVQIML NSEVVDIELD NQGHVTGVVY MDENGNRKIM KSHHVVFCSG GFGYSKEMLK
EYSPNLIHLP TTNGKQTTGD GQKILSKLGA ELIDMDQVQV HPTGFIDPND RENNWKFLAA
EALRGLGGIL LHPTTGRRFT NELSTRDTVT MEIQSKCPKN DNRALLVMSD KVYENYTNNI
NFYMSKNLIK KVSINDLIRQ YDLQTTASEL VTELKSYSDV NTKDTFDRPL IINAFDKDIS
TESTVYVGEV TPVVHFTMGG VKINEKSQVI KKNSESVLSN GIFAAGEVSG GVHGANRLGG
SSLLECVVFG KTAADNIAKL Y
