CBR4_BOVIN
ID CBR4_BOVIN Reviewed; 237 AA.
AC A4IFA7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase;
DE EC=1.1.1.100 {ECO:0000250|UniProtKB:Q8N4T8};
DE AltName: Full=3-ketoacyl-[acyl-carrier-protein] reductase beta subunit {ECO:0000250|UniProtKB:Q8N4T8};
DE Short=KAR beta subunit {ECO:0000250|UniProtKB:Q8N4T8};
DE AltName: Full=Carbonyl reductase family member 4;
DE Short=CBR4;
DE AltName: Full=Quinone reductase CBR4;
DE EC=1.6.5.10 {ECO:0000250|UniProtKB:Q8N4T8};
GN Name=CBR4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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. The homotetramer has NADPH-dependent quinone reductase
CC activity (in vitro), hence could play a role in protection against
CC cytotoxicity of exogenous quinones. As a heterotetramer, it can also
CC reduce 9,10-phenanthrenequinone, 1,4-benzoquinone and various other o-
CC quinones and p-quinones (in vitro). {ECO:0000250|UniProtKB:Q8N4T8}.
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:0000250|UniProtKB:Q8N4T8};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17399;
CC Evidence={ECO:0000250|UniProtKB:Q8N4T8};
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:0000250|UniProtKB:Q8N4T8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46165;
CC Evidence={ECO:0000250|UniProtKB:Q8N4T8};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:Q8N4T8}.
CC -!- SUBUNIT: Homotetramer (in vitro). Heterotetramer with HSD17B8; contains
CC two molecules each of HSD17B8 and CBR4. Does not form homotetramers
CC when HSD17B8 is coexpressed, only heterotetramers (in vitro).
CC {ECO:0000250|UniProtKB:Q8N4T8}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q8N4T8}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; BC134482; AAI34483.1; -; mRNA.
DR RefSeq; NP_001077186.1; NM_001083717.1.
DR AlphaFoldDB; A4IFA7; -.
DR SMR; A4IFA7; -.
DR STRING; 9913.ENSBTAP00000029363; -.
DR PaxDb; A4IFA7; -.
DR PeptideAtlas; A4IFA7; -.
DR PRIDE; A4IFA7; -.
DR Ensembl; ENSBTAT00000029363; ENSBTAP00000029363; ENSBTAG00000022013.
DR GeneID; 533020; -.
DR KEGG; bta:533020; -.
DR CTD; 84869; -.
DR VEuPathDB; HostDB:ENSBTAG00000022013; -.
DR VGNC; VGNC:26815; CBR4.
DR eggNOG; KOG1200; Eukaryota.
DR GeneTree; ENSGT00940000157620; -.
DR HOGENOM; CLU_010194_1_3_1; -.
DR InParanoid; A4IFA7; -.
DR OMA; KHMVDAG; -.
DR OrthoDB; 1226147at2759; -.
DR TreeFam; TF354265; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000022013; Expressed in metanephros cortex and 109 other tissues.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:1990204; C:oxidoreductase complex; ISS:UniProtKB.
DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; ISS:UniProtKB.
DR GO; GO:0070402; F:NADPH binding; IEA:Ensembl.
DR GO; GO:0008753; F:NADPH dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
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; IBA:GO_Central.
DR GO; GO:0044597; P:daunorubicin metabolic process; IEA:Ensembl.
DR GO; GO:0044598; P:doxorubicin metabolic process; IEA:Ensembl.
DR GO; GO:0006633; P:fatty acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Acetylation; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Mitochondrion; NAD; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..237
FT /note="3-oxoacyl-[acyl-carrier-protein] reductase"
FT /id="PRO_0000319877"
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:0000250|UniProtKB:Q8N4T8"
FT BINDING 34..35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8N4T8"
FT BINDING 56
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8N4T8"
FT BINDING 83..85
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8N4T8"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8N4T8"
FT BINDING 148
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8N4T8"
FT BINDING 152
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8N4T8"
FT BINDING 181..183
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8N4T8"
FT SITE 169
FT /note="Important for interaction with acyl carrier protein
FT (ACP)"
FT /evidence="ECO:0000250|UniProtKB:Q8N4T8"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8N4T8"
FT MOD_RES 195
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91VT4"
SQ SEQUENCE 237 AA; 25269 MW; 4499B1916326A968 CRC64;
MDKVCAVFGG SRGIGRAVAR LMAQRGYRLA IVARNLEGAR AAAGDLGGDH LALSCDVAKE
HDVQNTFEEI EKNLGRVNFL VNAAGINRDN LLVRTNTEDM LSQLHTNLLG SMLTCRAALK
TMIKQQRGSI VNVGSVVGLK GNSGQSVYSA SKGGLVGFSR ALAKEVAKKK IRVNVVAPGF
IHTDMTKDLN EELLKKNIPL GRFGDALDVA QAAVFLLESP YVTGHVLVVD GGLQLTM
