ID A0A3Q7TT52_VULVU Unreviewed; 435 AA.
AC A0A3Q7TT52;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
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};
GN Name=HIBCH {ECO:0000313|RefSeq:XP_025858440.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025858440.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025858440.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025858440.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025858440.1};
RG RefSeq;
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}.
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DR RefSeq; XP_025858440.1; XM_026002655.1.
DR AlphaFoldDB; A0A3Q7TT52; -.
DR STRING; 9627.ENSVVUP00000038154; -.
DR Ensembl; ENSVVUT00000050022; ENSVVUP00000038154; ENSVVUG00000027214.
DR KEGG; vvp:112922929; -.
DR OMA; EWEKSDM; -.
DR OrthoDB; 3639304at2759; -.
DR UniPathway; UPA00362; -.
DR Proteomes; UP000286640; 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; 1.
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:UP000286640}.
FT DOMAIN 96..425
FT /note="Enoyl-CoA hydratase/isomerase"
FT /evidence="ECO:0000259|Pfam:PF16113"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 435 AA; 48084 MW; 37DCF423EA4C9E9D CRC64;
MAAQSPGGRP CAPRSRRRLA RAAPARWGSG PRSSPGPAAP SPQRGRGPGP RRPVRSSLTC
RFNSFRRTNV ILQHLGMSKH TDAAGEVLLE RRGCAGVITL NRPKFLNALN LNMIRHIYPQ
LKNWEQDPET FLIIIKGAGG KAFCAGGDIR VISEGGKANQ KIAQDFFREE YMLNNAIDSC
RKPYVALIHG ITMGGGVGLS VHGQFRVATE KSLFAMPETA IGLFPDVGGG YFLPRLQGKL
GYFLALTGFR LKGRDVYAAG IATHFVDSEK LDMLEEDLLA LKSPSKENIA DVLDAYHTKS
KIDQDKSFIL EEHMDKINSW FSANTVEQII ENLQQDGSSF ALEQLKVINK MSPTSLKITV
RQLMEGSSKT LQEVLTMEYR LSQACVGGHD FHEGVRAVLI DKDQSPKWKP ADLKEVTDED
LNNYFKPLGS NDLKF
//