CBR4_HUMAN
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 03-AUG-2022, entry version 155.
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}.
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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; 51.
DR IntAct; Q8N4T8; 5.
DR STRING; 9606.ENSP00000303525; -.
DR iPTMnet; Q8N4T8; -.
DR PhosphoSitePlus; Q8N4T8; -.
DR BioMuta; CBR4; -.
DR DMDM; 269849708; -.
DR EPD; Q8N4T8; -.
DR jPOST; Q8N4T8; -.
DR MassIVE; Q8N4T8; -.
DR MaxQB; Q8N4T8; -.
DR PaxDb; Q8N4T8; -.
DR PeptideAtlas; Q8N4T8; -.
DR PRIDE; Q8N4T8; -.
DR ProteomicsDB; 71975; -. [Q8N4T8-1]
DR ProteomicsDB; 71976; -. [Q8N4T8-2]
DR Antibodypedia; 28439; 178 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 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; KHMVDAG; -.
DR OrthoDB; 1474004at2759; -.
DR PhylomeDB; Q8N4T8; -.
DR TreeFam; TF354265; -.
DR BioCyc; MetaCyc:ENSG00000145439-MON; -.
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; 11 hits in 1078 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 205 other tissues.
DR ExpressionAtlas; Q8N4T8; baseline and differential.
DR Genevisible; Q8N4T8; HS.
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 InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
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; 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 NADPH-
FT dependent reductase activity with acetoacetyl-CoA and 9,10-
FT phenanthrene quinone. No effect on NADH-dependent reductase
FT 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 NADPH-
FT 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 NADH-
FT 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
