FABG_YEAST
ID FABG_YEAST Reviewed; 278 AA.
AC P35731; D6VXN2;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase;
DE EC=1.1.1.100;
DE AltName: Full=3-ketoacyl-acyl carrier protein reductase;
GN Name=OAR1; OrderedLocusNames=YKL055C;
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=ATCC 204508 / S288c;
RX PubMed=8091862; DOI=10.1002/yea.320100008;
RA Rasmussen S.W.;
RT "Sequence of a 28.6 kb region of yeast chromosome XI includes the FBA1 and
RT TOA2 genes, an open reading frame (ORF) similar to a translationally
RT controlled tumour protein, one ORF containing motifs also found in plant
RT storage proteins and 13 ORFs with weak or no homology to known proteins.";
RL Yeast 10:S63-S68(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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.
RX PubMed=9388293; DOI=10.1007/s002940050292;
RA Schneider R., Brors B., Buerger F., Camrath S., Weiss H.;
RT "Two genes of the putative mitochondrial fatty acid synthase in the genome
RT of Saccharomyces cerevisiae.";
RL Curr. Genet. 32:384-388(1997).
RN [5]
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 [6]
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).
CC -!- FUNCTION: Involved in biosynthesis of fatty acids in mitochondria.
CC {ECO:0000250, ECO:0000269|PubMed:9388293}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
CC + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1760 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; X75781; CAA53417.1; -; Genomic_DNA.
DR EMBL; Z28055; CAA81892.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09102.1; -; Genomic_DNA.
DR PIR; S37877; S37877.
DR RefSeq; NP_012868.1; NM_001179621.2.
DR PDB; 4FD3; X-ray; 2.60 A; A/B/C/D/E/F=1-278.
DR PDB; 4FDA; X-ray; 2.10 A; A=1-273.
DR PDB; 4HBG; X-ray; 2.27 A; A=1-278.
DR PDBsum; 4FD3; -.
DR PDBsum; 4FDA; -.
DR PDBsum; 4HBG; -.
DR AlphaFoldDB; P35731; -.
DR SMR; P35731; -.
DR BioGRID; 34078; 416.
DR DIP; DIP-5403N; -.
DR IntAct; P35731; 1.
DR STRING; 4932.YKL055C; -.
DR MaxQB; P35731; -.
DR PaxDb; P35731; -.
DR PRIDE; P35731; -.
DR TopDownProteomics; P35731; -.
DR EnsemblFungi; YKL055C_mRNA; YKL055C; YKL055C.
DR GeneID; 853810; -.
DR KEGG; sce:YKL055C; -.
DR SGD; S000001538; OAR1.
DR VEuPathDB; FungiDB:YKL055C; -.
DR eggNOG; KOG0725; Eukaryota.
DR GeneTree; ENSGT00940000176504; -.
DR HOGENOM; CLU_010194_2_10_1; -.
DR InParanoid; P35731; -.
DR OMA; PSKCIIN; -.
DR BioCyc; MetaCyc:YKL055C-MON; -.
DR BioCyc; YEAST:YKL055C-MON; -.
DR BRENDA; 1.1.1.100; 984.
DR UniPathway; UPA00094; -.
DR PRO; PR:P35731; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P35731; protein.
DR GO; GO:0005739; C:mitochondrion; IMP:SGD.
DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IDA:SGD.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0009060; P:aerobic respiration; IMP:SGD.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006631; P:fatty acid metabolic process; IMP:SGD.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 2.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Mitochondrion; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..278
FT /note="3-oxoacyl-[acyl-carrier-protein] reductase"
FT /id="PRO_0000054872"
FT ACT_SITE 198
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 8..32
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:4FDA"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:4FDA"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:4FDA"
FT HELIX 38..42
FT /evidence="ECO:0007829|PDB:4FDA"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:4FDA"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:4FDA"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:4FDA"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:4FDA"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:4FDA"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:4FDA"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:4FDA"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:4FDA"
FT STRAND 108..119
FT /evidence="ECO:0007829|PDB:4FDA"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:4FDA"
FT HELIX 134..144
FT /evidence="ECO:0007829|PDB:4FDA"
FT HELIX 146..165
FT /evidence="ECO:0007829|PDB:4FDA"
FT HELIX 167..171
FT /evidence="ECO:0007829|PDB:4FDA"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:4FD3"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:4FDA"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:4FDA"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:4FDA"
FT HELIX 196..216
FT /evidence="ECO:0007829|PDB:4FDA"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:4FDA"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:4FDA"
FT HELIX 246..251
FT /evidence="ECO:0007829|PDB:4HBG"
FT HELIX 260..272
FT /evidence="ECO:0007829|PDB:4FDA"
SQ SEQUENCE 278 AA; 31184 MW; 62FC3BC347D3E933 CRC64;
MHYLPVAIVT GATRGIGKAI CQKLFQKGLS CIILGSTKES IERTAIDRGQ LQSGLSYQRQ
CAIAIDFKKW PHWLDYESYD GIEYFKDRPP LKQKYSTLFD PCNKWSNNER RYYVNLLINC
AGLTQESLSV RTTASQIQDI MNVNFMSPVT MTNICIKYMM KSQRRWPELS GQSARPTIVN
ISSILHSGKM KVPGTSVYSA SKAALSRFTE VLAAEMEPRN IRCFTISPGL VKGTDMIQNL
PVEAKEMLER TIGASGTSAP AEIAEEVWSL YSRTALET
