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 27-MAR-2024, entry version 102.
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; 7955-ENSDARP00000010074; -.
DR AGR; ZFIN:ZDB-GENE-040426-1796; -.
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 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 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.
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
//
