CBR4_XENTR
ID CBR4_XENTR Reviewed; 236 AA.
AC Q68ER2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
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;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-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; BC080139; AAH80139.1; -; mRNA.
DR RefSeq; NP_001007873.1; NM_001007872.1.
DR RefSeq; XP_012815703.1; XM_012960249.2.
DR RefSeq; XP_012815704.1; XM_012960250.2.
DR RefSeq; XP_012815711.1; XM_012960257.2.
DR AlphaFoldDB; Q68ER2; -.
DR SMR; Q68ER2; -.
DR STRING; 8364.ENSXETP00000010799; -.
DR PaxDb; Q68ER2; -.
DR DNASU; 493259; -.
DR Ensembl; ENSXETT00000010799; ENSXETP00000010799; ENSXETG00000004944.
DR GeneID; 493259; -.
DR KEGG; xtr:493259; -.
DR CTD; 84869; -.
DR eggNOG; KOG1200; Eukaryota.
DR HOGENOM; CLU_010194_1_3_1; -.
DR InParanoid; Q68ER2; -.
DR OMA; AKDANTM; -.
DR OrthoDB; 1226147at2759; -.
DR PhylomeDB; Q68ER2; -.
DR TreeFam; TF354265; -.
DR Reactome; R-XTR-75105; Fatty acyl-CoA biosynthesis.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000004944; Expressed in testis and 13 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: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..236
FT /note="Carbonyl reductase family member 4"
FT /id="PRO_0000319883"
FT ACT_SITE 147
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 55
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8N4T8"
FT BINDING 82..84
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8N4T8"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8N4T8"
FT BINDING 147
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8N4T8"
FT BINDING 151
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8N4T8"
FT BINDING 180..182
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8N4T8"
SQ SEQUENCE 236 AA; 25219 MW; 6623A4A57601C267 CRC64;
MTKVCAVFGG SRGIGKAVSK LLAQRDYKVA VISRDLEVAK AAAAEVGAHL ALSCDVSKEN
EIQDTFKEIT NNLGNVDYLV NSAGIRRDAL LLRTRSEDIR SLLSVNLVGT IQTCKLALRS
MIQQQGGAIV NIGSIVGHKG NIGQSIYGAS KEGLIGFSKS LAKEVAKRNI RVNVVAPGFI
HTDMTLGLEE DSLTKMVPLG RFGDPEEVAQ SVLFLLESPY ITGHVLVVDG GLQLQM
