ID   CBR4_DANRE              Reviewed;         237 AA.
AC   Q6P0H7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Carbonyl reductase family member 4;
DE            EC=1.-.-.-;
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=3-oxoacyl-[acyl-carrier-protein] reductase;
DE            EC=1.1.1.- {ECO:0000250|UniProtKB:Q8N4T8};
DE   AltName: Full=Quinone reductase CBR4;
GN   Name=cbr4; ORFNames=zgc:77144;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The heterotetramer with HSD17B8 has NADH-dependent 3-
CC       ketoacyl-acyl carrier protein reductase activity, and thereby plays a
CC       role in mitochondrial fatty acid biosynthesis. Within the
CC       heterotetramer, HSD17B8 binds NADH; CBR4 binds NADPD. The homotetramer
CC       has NADPH-dependent quinone reductase activity. Both homotetramer and
CC       the heterotetramer have broad in vitro substrate specificity and can
CC       reduce 9,10-phenanthrenequinone, 1,4-benzoquinone and various other o-
CC       quinones and p-quinones. {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. {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; BC065615; AAH65615.1; -; mRNA.
DR   AlphaFoldDB; Q6P0H7; -.
DR   SMR; Q6P0H7; -.
DR   STRING; 7955.ENSDARP00000010074; -.
DR   PaxDb; Q6P0H7; -.
DR   ZFIN; ZDB-GENE-040426-1796; cbr4.
DR   eggNOG; KOG1200; Eukaryota.
DR   InParanoid; Q6P0H7; -.
DR   PhylomeDB; Q6P0H7; -.
DR   Reactome; R-DRE-75105; Fatty acyl-CoA biosynthesis.
DR   UniPathway; UPA00094; -.
DR   PRO; PR:Q6P0H7; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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: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:0006633; P:fatty acid biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0051290; P:protein heterotetramerization; ISS: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   2: Evidence at transcript level;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; Mitochondrion; NAD; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..237
FT                   /note="Carbonyl reductase family member 4"
FT                   /id="PRO_0000319881"
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         57
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N4T8"
FT   BINDING         84..86
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"
SQ   SEQUENCE   237 AA;  24879 MW;  19ED5825EDDD8E41 CRC64;
     MSRLAVVFGG SRGIGRAASK LLAQRGHRIV LLSRNKEAAQ STAQSLPGEN HLGLSCDVSK
     EEEVQKAFET INKTCGTVGF LVNAAGINRD ALLLRSKSED MLSVLHTNLL GSMLTCKAAV
     RNMLSHGGAI VNIGSVVGVK GNAGQCVYSA SKAGLEGFTR SLAKEVASRN IRVNLVAPGL
     IHTDMTAGLA EEAAVRTIPL GRFGEPAEVA QAMLFLLESP YITGQILLVD GGLQLLM