CEM1_YEAST
ID CEM1_YEAST Reviewed; 442 AA.
AC P39525; D3DLW6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase homolog;
DE EC=2.3.1.41;
DE AltName: Full=Beta-ketoacyl-ACP synthase homolog;
GN Name=CEM1; OrderedLocusNames=YER061C;
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].
RC STRAIN=CW04;
RX PubMed=8412701; DOI=10.1111/j.1365-2958.1993.tb01715.x;
RA Harington A., Herbert C.J., Tung B., Getz G.S., Slonimski P.P.;
RT "Identification of a new nuclear gene (CEM1) encoding a protein homologous
RT to a beta-keto-acyl synthase which is essential for mitochondrial
RT respiration in Saccharomyces cerevisiae.";
RL Mol. Microbiol. 9:545-555(1993).
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
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 [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
CC -!- FUNCTION: Possibly involved in the synthesis of a specialized molecule,
CC probably related to a fatty acid, which is essential for mitochondrial
CC respiration. Is essential for oxygen uptake and the presence of
CC cytochromes A and B.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP]
CC + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC EC=2.3.1.41;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16823961}.
CC -!- MISCELLANEOUS: Present with 1660 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {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; X73488; CAB58180.1; -; Genomic_DNA.
DR EMBL; U18813; AAB64597.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07720.2; -; Genomic_DNA.
DR PIR; S36204; S36204.
DR RefSeq; NP_010983.2; NM_001178952.2.
DR AlphaFoldDB; P39525; -.
DR SMR; P39525; -.
DR BioGRID; 36803; 502.
DR DIP; DIP-5342N; -.
DR IntAct; P39525; 2.
DR MINT; P39525; -.
DR STRING; 4932.YER061C; -.
DR MaxQB; P39525; -.
DR PaxDb; P39525; -.
DR PRIDE; P39525; -.
DR EnsemblFungi; YER061C_mRNA; YER061C; YER061C.
DR GeneID; 856790; -.
DR KEGG; sce:YER061C; -.
DR SGD; S000000863; CEM1.
DR VEuPathDB; FungiDB:YER061C; -.
DR eggNOG; KOG1394; Eukaryota.
DR GeneTree; ENSGT00940000157768; -.
DR HOGENOM; CLU_000022_69_2_1; -.
DR InParanoid; P39525; -.
DR OMA; QIGHCLG; -.
DR BioCyc; MetaCyc:YER061C-MON; -.
DR BioCyc; YEAST:YER061C-MON; -.
DR PRO; PR:P39525; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P39525; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; ISA:SGD.
DR GO; GO:0006633; P:fatty acid biosynthetic process; ISA:SGD.
DR CDD; cd00834; KAS_I_II; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR000794; Beta-ketoacyl_synthase.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR11712; PTHR11712; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Mitochondrion; Reference proteome; Transferase.
FT CHAIN 1..442
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase homolog"
FT /id="PRO_0000180356"
FT ACT_SITE 187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
SQ SEQUENCE 442 AA; 47555 MW; DAF2FF358A7AA067 CRC64;
MSRRVVITGL GCVTPLGRSL SESWGNLLSS KNGLTPITSL PNYNEDYKLR EKSIPSTITV
GKIPENFQNE NSAINKLLFT SQDERRTSSF IKLALRTTYE ALHNAGLLNP NDITINTSLC
NLDHFGCLIG SGIGSIQDIY QTSLQFHNDN KRINPYFVPK ILTNMAAGNV SIKFNLRGLS
HSVSTACATG NNSIGDAFNF IRLGMQDICV AGASETSLHP LSLAGFIRAK SITTNGISRP
FDTQRSGFVL GEGCGMIVME SLEHAQKRNA NIISELVGYG LSSDACHITS PPADGNGAKR
AIEMALKMAR LEPTDVDYVN AHATSTLLGD KAECLAVASA LLPGRSKSKP LYISSNKGAI
GHLLGAAGAV ESIFTICSLK DDKMPHTLNL DNVLTLENNE ADKLHFIRDK PIVGANPKYA
LCNSFGFGGV NTSLLFKKWE GS
