GenomeNet

Database: UniProt
Entry: A0A3Q2X525_HAPBU
LinkDB: A0A3Q2X525_HAPBU
Original site: A0A3Q2X525_HAPBU 
ID   A0A3Q2X525_HAPBU        Unreviewed;       368 AA.
AC   A0A3Q2X525;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=3-hydroxyisobutyryl-CoA hydrolase {ECO:0000256|RuleBase:RU369070};
DE            Short=HIB-CoA hydrolase {ECO:0000256|RuleBase:RU369070};
DE            Short=HIBYL-CoA-H {ECO:0000256|RuleBase:RU369070};
DE            EC=3.1.2.4 {ECO:0000256|RuleBase:RU369070};
DE   AltName: Full=3-hydroxyisobutyryl-coenzyme A hydrolase {ECO:0000256|RuleBase:RU369070};
OS   Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000034789.1, ECO:0000313|Proteomes:UP000264840};
RN   [1] {ECO:0000313|Ensembl:ENSHBUP00000034789.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00024871}.
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         Evidence={ECO:0000256|ARBA:ARBA00001709,
CC         ECO:0000256|RuleBase:RU369070};
CC   -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC       {ECO:0000256|ARBA:ARBA00005109, ECO:0000256|RuleBase:RU369070}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|RuleBase:RU369070}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000256|ARBA:ARBA00005254, ECO:0000256|RuleBase:RU369070}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_005939914.1; XM_005939852.1.
DR   AlphaFoldDB; A0A3Q2X525; -.
DR   Ensembl; ENSHBUT00000029917.1; ENSHBUP00000034789.1; ENSHBUG00000022595.1.
DR   GeneTree; ENSGT00890000139491; -.
DR   OrthoDB; 3639304at2759; -.
DR   UniPathway; UPA00362; -.
DR   Proteomes; UP000264840; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0003860; F:3-hydroxyisobutyryl-CoA hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006574; P:valine catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06558; crotonase-like; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR045004; ECH_dom.
DR   InterPro; IPR032259; HIBYL-CoA-H.
DR   PANTHER; PTHR43176:SF3; 3-HYDROXYISOBUTYRYL-COA HYDROLASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43176; 3-HYDROXYISOBUTYRYL-COA HYDROLASE-RELATED; 1.
DR   Pfam; PF16113; ECH_2; 2.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
PE   3: Inferred from homology;
KW   Branched-chain amino acid catabolism {ECO:0000256|ARBA:ARBA00022456};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU369070};
KW   Mitochondrion {ECO:0000256|RuleBase:RU369070};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264840}.
FT   DOMAIN          43..169
FT                   /note="Enoyl-CoA hydratase/isomerase"
FT                   /evidence="ECO:0000259|Pfam:PF16113"
FT   DOMAIN          203..358
FT                   /note="Enoyl-CoA hydratase/isomerase"
FT                   /evidence="ECO:0000259|Pfam:PF16113"
FT   REGION          179..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..193
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   368 AA;  40736 MW;  7E5D627A8DA74D88 CRC64;
     MSLTVLTSAY RLRSLCRLQR IQAHMMSSHA EPEVLLEKVG RTGVITMNRP KVLNALNLTM
     IRQIYPQLKK WESDNETDIV IIKGAGDKAF CAGGDIRAVT EAGKVGDSLA QDFFREEYIL
     NNAIGSYRKP YIALIDGITM GGGVGLSVHG RFRVATEKTL FAMPETAIAS REIGKQTHCI
     TQRGRDRSRT SNSHRAGKAN ALQIPDLQKE LVDLKSPSAE DVSRVLDSYQ SQSSLDAEKP
     FILKKHVSDI DRLFSASSVE GIVKNLKTDG SEFAKKQTET LSKMSPTSLK ITLKQLQAGA
     ALSLQDVLVM EYRLSQACMR GCDFYEGVRA VLVDKDQNPK WNPSTLEEVS DQMVEQCFSS
     LGEKDLTL
//
DBGET integrated database retrieval system