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HIBCH_DANRE
ID   HIBCH_DANRE             Reviewed;         382 AA.
AC   Q58EB4;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=3-hydroxyisobutyryl-CoA hydrolase, mitochondrial;
DE            EC=3.1.2.4;
DE   AltName: Full=3-hydroxyisobutyryl-coenzyme A hydrolase;
DE            Short=HIB-CoA hydrolase;
DE            Short=HIBYL-CoA-H;
DE   Flags: Precursor;
GN   Name=hibch; ORFNames=zgc:110824;
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=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline
CC       catabolite. Has high activity toward isobutyryl-CoA. Could be an
CC       isobutyryl-CoA dehydrogenase that functions in valine catabolism. Also
CC       hydrolyzes 3-hydroxypropanoyl-CoA (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-hydroxy-2-methylpropanoyl-CoA + H2O = 3-hydroxy-2-
CC         methylpropanoate + CoA + H(+); Xref=Rhea:RHEA:20888,
CC         ChEBI:CHEBI:11805, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57340; EC=3.1.2.4;
CC   -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; BC091995; AAH91995.1; -; mRNA.
DR   RefSeq; NP_001014338.1; NM_001014316.1.
DR   AlphaFoldDB; Q58EB4; -.
DR   SMR; Q58EB4; -.
DR   STRING; 7955.ENSDARP00000118435; -.
DR   PaxDb; Q58EB4; -.
DR   PeptideAtlas; Q58EB4; -.
DR   PRIDE; Q58EB4; -.
DR   GeneID; 798364; -.
DR   KEGG; dre:798364; -.
DR   CTD; 26275; -.
DR   ZFIN; ZDB-GENE-050327-29; hibch.
DR   eggNOG; KOG1684; Eukaryota.
DR   InParanoid; Q58EB4; -.
DR   OrthoDB; 1369862at2759; -.
DR   Reactome; R-DRE-70895; Branched-chain amino acid catabolism.
DR   UniPathway; UPA00362; -.
DR   ChiTaRS; hibch; zebrafish.
DR   PRO; PR:Q58EB4; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0003860; F:3-hydroxyisobutyryl-CoA hydrolase activity; IBA:GO_Central.
DR   GO; GO:0006574; P:valine catabolic process; IBA:GO_Central.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR045004; ECH_dom.
DR   InterPro; IPR032259; HIBYL-CoA-H.
DR   PANTHER; PTHR43176; PTHR43176; 1.
DR   Pfam; PF16113; ECH_2; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
PE   2: Evidence at transcript level;
KW   Branched-chain amino acid catabolism; Hydrolase; Mitochondrion;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..382
FT                   /note="3-hydroxyisobutyryl-CoA hydrolase, mitochondrial"
FT                   /id="PRO_0000284933"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   382 AA;  42277 MW;  33E9124B82D1C66D CRC64;
     MSLIIFTSAQ RLRSVCRLQR IHGHMMSSKA GSEVLFEKVG KAGVITLNRP KALNALTLNM
     IRHIYPQLKK WDKDSETDIV IIKGAGEKAF CAGGDIRAIA EAGKAGNLLS QVFFREEYIL
     NNTIGTYQKP YVALINGITM GGGVGLSVHG QFRVATEKTL FAMPETGIGL FPDVGGGYFL
     PRLQGKLGLF LALTGFRLKG RDVQRVGVAT HFVQSEKIES LEKDLVDLKS PSISDVAQLL
     DSYQEQSHLD AEKPFVLQEQ TEAIDRLFSA GSVEEIVENL KKDGSAFALK QAETLAKMSP
     TSLKLTFRQI EEGARMSLQE VFMMEYRLSQ ACMNGHDFYE GVRAVLIDKD QSPKWKPSTL
     AGVSEQFVDK CFSSLDERDL KL
 
 
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