ID CBR4_HUMAN Reviewed; 237 AA. AC Q8N4T8; Q8WTW8; Q96K93; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 24-NOV-2009, sequence version 3. DT 27-MAR-2024, entry version 164. DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase; DE EC=1.1.1.100 {ECO:0000269|PubMed:25203508}; DE AltName: Full=3-ketoacyl-[acyl-carrier-protein] reductase beta subunit {ECO:0000303|PubMed:25203508}; DE Short=KAR beta subunit {ECO:0000303|PubMed:25203508}; DE AltName: Full=Carbonyl reductase family member 4; DE Short=CBR4 {ECO:0000303|PubMed:19000905, ECO:0000303|PubMed:19571038, ECO:0000303|PubMed:25203508}; DE AltName: Full=Quinone reductase CBR4 {ECO:0000305|PubMed:19000905}; DE EC=1.6.5.10 {ECO:0000269|PubMed:19000905}; DE AltName: Full=Short chain dehydrogenase/reductase family 45C member 1; GN Name=CBR4; Synonyms=SDR45C1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP MET-70. RC TISSUE=Embryo, and Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-70. RC TISSUE=Melanoma; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-70. RC TISSUE=Duodenum, and Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, RP SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE RP SPECIFICITY. RX PubMed=19000905; DOI=10.1016/j.bbrc.2008.11.003; RA Endo S., Matsunaga T., Kitade Y., Ohno S., Tajima K., El-Kabbani O., RA Hara A.; RT "Human carbonyl reductase 4 is a mitochondrial NADPH-dependent quinone RT reductase."; RL Biochem. Biophys. Res. Commun. 377:1326-1330(2008). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HSD17B8, AND PATHWAY. RX PubMed=19571038; DOI=10.1096/fj.09-133587; RA Chen Z., Kastaniotis A.J., Miinalainen I.J., Rajaram V., Wierenga R.K., RA Hiltunen J.K.; RT "17beta-Hydroxysteroid dehydrogenase type 8 and carbonyl reductase type 4 RT assemble as a ketoacyl reductase of human mitochondrial FAS."; RL FASEB J. 23:3682-3691(2009). RN [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS) IN COMPLEX WITH NADP AND HSD17B8, RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH HSD17B8, SUBUNIT, PATHWAY, RP AND MUTAGENESIS OF GLY-9; ARG-12; ARG-34; SER-135; TYR-148; LYS-152; RP ARG-168 AND LYS-169. RX PubMed=25203508; DOI=10.1038/ncomms5805; RA Venkatesan R., Sah-Teli S.K., Awoniyi L.O., Jiang G., Prus P., RA Kastaniotis A.J., Hiltunen J.K., Wierenga R.K., Chen Z.; RT "Insights into mitochondrial fatty acid synthesis from the structure of RT heterotetrameric 3-ketoacyl-ACP reductase/3R-hydroxyacyl-CoA RT dehydrogenase."; RL Nat. Commun. 5:4805-4805(2014). RN [11] RP VARIANT [LARGE SCALE ANALYSIS] MET-70, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). CC -!- FUNCTION: Component of the heterotetramer complex KAR (3-ketoacyl-[acyl CC carrier protein] reductase or 3-ketoacyl-[ACP] reductase) that forms CC part of the mitochondrial fatty acid synthase (mtFAS). Beta-subunit of CC the KAR heterotetramer complex, responsible for the 3-ketoacyl-ACP CC reductase activity of the mtFAS, reduces 3-oxoacyl-[ACP] to (3R)- CC hydroxyacyl-[ACP] in a NADPH-dependent manner with no chain length CC preference, thereby participating in mitochondrial fatty acid CC biosynthesis (PubMed:25203508). The homotetramer has NADPH-dependent CC quinone reductase activity (in vitro), hence could play a role in CC protection against cytotoxicity of exogenous quinones CC (PubMed:19000905). As a heterotetramer, it can also reduce 9,10- CC phenanthrenequinone, 1,4-benzoquinone and various other o-quinones and CC p-quinones (in vitro) (PubMed:19000905, PubMed:19571038, CC PubMed:25203508). {ECO:0000269|PubMed:19000905, CC ECO:0000269|PubMed:19571038, ECO:0000269|PubMed:25203508}. 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 Evidence={ECO:0000269|PubMed:25203508}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17399; CC Evidence={ECO:0000269|PubMed:25203508}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a quinone + H(+) + NADPH = a quinol + NADP(+); CC Xref=Rhea:RHEA:46164, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132124; CC EC=1.6.5.10; Evidence={ECO:0000269|PubMed:19000905}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46165; CC Evidence={ECO:0000269|PubMed:19000905}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=11 uM for NADPH (with homotetramer) {ECO:0000269|PubMed:19000905}; CC KM=1.6 uM for 9,10-phenanthroquinone (with homotetramer) CC {ECO:0000269|PubMed:19000905}; CC KM=1.9 uM for 1,4-benzoquinone (with homotetramer) CC {ECO:0000269|PubMed:19000905}; CC pH dependence: CC Optimum pH is 6-8 (with homotetramer). {ECO:0000269|PubMed:19000905}; CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC {ECO:0000269|PubMed:19571038, ECO:0000269|PubMed:25203508}. CC -!- SUBUNIT: Homotetramer (in vitro) (PubMed:19000905). Heterotetramer with CC HSD17B8; contains two molecules each of HSD17B8 and CBR4 CC (PubMed:19571038, PubMed:25203508). Does not form homotetramers when CC HSD17B8 is coexpressed, only heterotetramers (in vitro) CC (PubMed:25203508). {ECO:0000269|PubMed:19000905, CC ECO:0000269|PubMed:19571038, ECO:0000269|PubMed:25203508}. CC -!- INTERACTION: CC Q8N4T8; Q2QGD7: ZXDC; NbExp=3; IntAct=EBI-10897344, EBI-1538838; CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix CC {ECO:0000269|PubMed:19000905, ECO:0000269|PubMed:19571038}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8N4T8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8N4T8-2; Sequence=VSP_031527; CC -!- TISSUE SPECIFICITY: Detected in liver and kidney (at protein level) CC (PubMed:19000905). Displays the highest expression in neuronal and CC muscle tissues (PubMed:25203508). {ECO:0000269|PubMed:19000905, CC ECO:0000303|PubMed:25203508}. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) CC 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; AK027337; BAB55045.1; -; mRNA. DR EMBL; AK291756; BAF84445.1; -; mRNA. DR EMBL; AL833393; CAH10582.1; -; mRNA. DR EMBL; AC021151; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471056; EAX04797.1; -; Genomic_DNA. DR EMBL; BC021973; AAH21973.1; -; mRNA. DR EMBL; BC033650; AAH33650.1; -; mRNA. DR CCDS; CCDS3812.1; -. [Q8N4T8-1] DR RefSeq; NP_116172.2; NM_032783.4. [Q8N4T8-1] DR PDB; 4CQL; X-ray; 2.85 A; B/C/F/G/J/K/N/O=1-237. DR PDB; 4CQM; X-ray; 2.34 A; B/C/F/G/J/K/N/O=1-237. DR PDBsum; 4CQL; -. DR PDBsum; 4CQM; -. DR AlphaFoldDB; Q8N4T8; -. DR SMR; Q8N4T8; -. DR BioGRID; 124314; 54. DR ComplexPortal; CPX-949; Mitochondrial 3-oxoacyl-[acyl-carrier-protein] reductase. DR IntAct; Q8N4T8; 6. DR MINT; Q8N4T8; -. DR STRING; 9606.ENSP00000303525; -. DR iPTMnet; Q8N4T8; -. DR PhosphoSitePlus; Q8N4T8; -. DR SwissPalm; Q8N4T8; -. DR BioMuta; CBR4; -. DR DMDM; 269849708; -. DR EPD; Q8N4T8; -. DR jPOST; Q8N4T8; -. DR MassIVE; Q8N4T8; -. DR MaxQB; Q8N4T8; -. DR PaxDb; 9606-ENSP00000303525; -. DR PeptideAtlas; Q8N4T8; -. DR ProteomicsDB; 71975; -. [Q8N4T8-1] DR ProteomicsDB; 71976; -. [Q8N4T8-2] DR Pumba; Q8N4T8; -. DR Antibodypedia; 28439; 195 antibodies from 24 providers. DR DNASU; 84869; -. DR Ensembl; ENST00000306193.8; ENSP00000303525.3; ENSG00000145439.12. [Q8N4T8-1] DR Ensembl; ENST00000504480.5; ENSP00000427615.1; ENSG00000145439.12. [Q8N4T8-2] DR GeneID; 84869; -. DR KEGG; hsa:84869; -. DR MANE-Select; ENST00000306193.8; ENSP00000303525.3; NM_032783.5; NP_116172.2. DR UCSC; uc003iry.4; human. [Q8N4T8-1] DR AGR; HGNC:25891; -. DR CTD; 84869; -. DR DisGeNET; 84869; -. DR GeneCards; CBR4; -. DR HGNC; HGNC:25891; CBR4. DR HPA; ENSG00000145439; Low tissue specificity. DR MIM; 619394; gene. DR neXtProt; NX_Q8N4T8; -. DR OpenTargets; ENSG00000145439; -. DR PharmGKB; PA144596471; -. DR VEuPathDB; HostDB:ENSG00000145439; -. DR eggNOG; KOG1200; Eukaryota. DR GeneTree; ENSGT00940000157620; -. DR HOGENOM; CLU_010194_1_3_1; -. DR InParanoid; Q8N4T8; -. DR OMA; CQKHMVD; -. DR OrthoDB; 5478123at2759; -. DR PhylomeDB; Q8N4T8; -. DR TreeFam; TF354265; -. DR BioCyc; MetaCyc:ENSG00000145439-MONOMER; -. DR PathwayCommons; Q8N4T8; -. DR Reactome; R-HSA-75105; Fatty acyl-CoA biosynthesis. DR SABIO-RK; Q8N4T8; -. DR SignaLink; Q8N4T8; -. DR UniPathway; UPA00094; -. DR BioGRID-ORCS; 84869; 13 hits in 1159 CRISPR screens. DR ChiTaRS; CBR4; human. DR GenomeRNAi; 84869; -. DR Pharos; Q8N4T8; Tbio. DR PRO; PR:Q8N4T8; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q8N4T8; Protein. DR Bgee; ENSG00000145439; Expressed in secondary oocyte and 207 other cell types or tissues. DR ExpressionAtlas; Q8N4T8; baseline and differential. DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB. DR GO; GO:1990204; C:oxidoreductase complex; IDA:UniProtKB. DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IDA:UniProtKB. DR GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IDA:UniProtKB. DR GO; GO:0070402; F:NADPH binding; IDA:UniProtKB. DR GO; GO:0008753; F:NADPH dehydrogenase (quinone) activity; IDA:UniProtKB. 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:0048038; F:quinone binding; IDA:UniProtKB. DR GO; GO:0044597; P:daunorubicin metabolic process; IMP:UniProtKB. DR GO; GO:0044598; P:doxorubicin metabolic process; IMP:UniProtKB. DR GO; GO:0006633; P:fatty acid biosynthetic process; IMP:UniProtKB. DR GO; GO:0051290; P:protein heterotetramerization; IDA:UniProtKB. DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR InterPro; IPR002347; SDR_fam. DR PANTHER; PTHR42760:SF40; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] REDUCTASE; 1. DR PANTHER; PTHR42760; SHORT-CHAIN DEHYDROGENASES/REDUCTASES FAMILY MEMBER; 1. DR Pfam; PF13561; adh_short_C2; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR SMART; SM00822; PKS_KR; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00061; ADH_SHORT; 1. DR Genevisible; Q8N4T8; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Fatty acid biosynthesis; KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Mitochondrion; KW NAD; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1..237 FT /note="3-oxoacyl-[acyl-carrier-protein] reductase" FT /id="PRO_0000319878" FT ACT_SITE 148 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001" FT BINDING 11..14 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:25203508, FT ECO:0007744|PDB:4CQM" FT BINDING 34..35 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:25203508, FT ECO:0007744|PDB:4CQM" FT BINDING 56 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:25203508, FT ECO:0007744|PDB:4CQM" FT BINDING 83..85 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:25203508, FT ECO:0007744|PDB:4CQM" FT BINDING 135 FT /ligand="substrate" FT /evidence="ECO:0000305|PubMed:25203508" FT BINDING 148 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:25203508, FT ECO:0007744|PDB:4CQM" FT BINDING 152 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:25203508, FT ECO:0007744|PDB:4CQM" FT BINDING 181..183 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:25203508, FT ECO:0007744|PDB:4CQM" FT SITE 169 FT /note="Important for interaction with acyl carrier protein FT (ACP)" FT /evidence="ECO:0000305|PubMed:25203508" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 40 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q91VT4" FT MOD_RES 96 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q91VT4" FT MOD_RES 195 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q91VT4" FT VAR_SEQ 180..237 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_031527" FT VARIANT 70 FT /note="L -> M (in dbSNP:rs2877380)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005, FT ECO:0007744|PubMed:21269460" FT /id="VAR_039049" FT MUTAGEN 9 FT /note="G->S: Unable to restore growth of an OAR1-deficient FT yeast mutant." FT /evidence="ECO:0000269|PubMed:25203508" FT MUTAGEN 12 FT /note="R->A: Strongly reduced ability to restore growth of FT an OAR1-deficient yeast mutant." FT /evidence="ECO:0000269|PubMed:25203508" FT MUTAGEN 34 FT /note="R->A: Strongly reduced ability to restore growth of FT an OAR1-deficient yeast mutant. Strongly reduces FT NADPH-dependent reductase activity with acetoacetyl-CoA and FT 9,10-phenanthrene quinone. No effect on NADH-dependent FT reductase activities." FT /evidence="ECO:0000269|PubMed:25203508" FT MUTAGEN 135 FT /note="S->A: Unable to restore growth of an OAR1-deficient FT yeast mutant." FT /evidence="ECO:0000269|PubMed:25203508" FT MUTAGEN 148 FT /note="Y->A: Unable to restore growth of an OAR1-deficient FT yeast mutant." FT /evidence="ECO:0000269|PubMed:25203508" FT MUTAGEN 152 FT /note="K->A: Unable to restore growth of an OAR1-deficient FT yeast mutant. Abolishes NADPH-dependent reductase activity FT with acetoacetyl-CoA. Strongly reduces NADPH-dependent FT reductase activity with 9,10-phenanthrene quinone. No FT effect on NADH-dependent reductase activities." FT /evidence="ECO:0000269|PubMed:25203508" FT MUTAGEN 168 FT /note="R->E: Strongly reduced ability to restore growth of FT an OAR1-deficient yeast mutant. Increases NADPH-dependent FT reductase activity with acetoacetyl-CoA. Reduces FT NADPH-dependent reductase activity with 9,10-phenanthrene FT quinone. No effect on NADH-dependent reductase activities." FT /evidence="ECO:0000269|PubMed:25203508" FT MUTAGEN 169 FT /note="K->E: Unable to restore growth of an OAR1-deficient FT yeast mutant. Increases NADPH-dependent reductase activity FT with acetoacetyl-CoA. Reduces NADPH-dependent reductase FT activity with 9,10-phenanthrene quinone. No effect on FT NADH-dependent reductase activities." FT /evidence="ECO:0000269|PubMed:25203508" FT STRAND 4..8 FT /evidence="ECO:0007829|PDB:4CQM" FT TURN 9..11 FT /evidence="ECO:0007829|PDB:4CQM" FT HELIX 14..23 FT /evidence="ECO:0007829|PDB:4CQM" FT TURN 24..26 FT /evidence="ECO:0007829|PDB:4CQM" FT STRAND 28..34 FT /evidence="ECO:0007829|PDB:4CQM" FT HELIX 36..45 FT /evidence="ECO:0007829|PDB:4CQM" FT STRAND 51..54 FT /evidence="ECO:0007829|PDB:4CQM" FT HELIX 60..69 FT /evidence="ECO:0007829|PDB:4CQM" FT TURN 70..74 FT /evidence="ECO:0007829|PDB:4CQM" FT STRAND 77..82 FT /evidence="ECO:0007829|PDB:4CQM" FT TURN 92..94 FT /evidence="ECO:0007829|PDB:4CQL" FT HELIX 97..107 FT /evidence="ECO:0007829|PDB:4CQM" FT HELIX 109..124 FT /evidence="ECO:0007829|PDB:4CQM" FT STRAND 128..133 FT /evidence="ECO:0007829|PDB:4CQM" FT HELIX 136..138 FT /evidence="ECO:0007829|PDB:4CQM" FT HELIX 146..165 FT /evidence="ECO:0007829|PDB:4CQM" FT HELIX 167..169 FT /evidence="ECO:0007829|PDB:4CQM" FT STRAND 171..178 FT /evidence="ECO:0007829|PDB:4CQM" FT HELIX 190..193 FT /evidence="ECO:0007829|PDB:4CQL" FT HELIX 206..218 FT /evidence="ECO:0007829|PDB:4CQM" FT STRAND 226..232 FT /evidence="ECO:0007829|PDB:4CQM" FT HELIX 233..235 FT /evidence="ECO:0007829|PDB:4CQM" SQ SEQUENCE 237 AA; 25301 MW; 376FF5FA0CB9ABF0 CRC64; MDKVCAVFGG SRGIGRAVAQ LMARKGYRLA VIARNLEGAK AAAGDLGGDH LAFSCDVAKE HDVQNTFEEL EKHLGRVNFL VNAAGINRDG LLVRTKTEDM VSQLHTNLLG SMLTCKAAMR TMIQQQGGSI VNVGSIVGLK GNSGQSVYSA SKGGLVGFSR ALAKEVARKK IRVNVVAPGF VHTDMTKDLK EEHLKKNIPL GRFGETIEVA HAVVFLLESP YITGHVLVVD GGLQLIL //