HIBCH_BOVIN
ID HIBCH_BOVIN Reviewed; 386 AA.
AC Q2HJ73;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) 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; BC113274; AAI13275.1; -; mRNA.
DR RefSeq; XP_010800133.1; XM_010801831.1.
DR RefSeq; XP_015317723.1; XM_015462237.1.
DR AlphaFoldDB; Q2HJ73; -.
DR SMR; Q2HJ73; -.
DR PeptideAtlas; Q2HJ73; -.
DR PRIDE; Q2HJ73; -.
DR InParanoid; Q2HJ73; -.
DR OrthoDB; 1369862at2759; -.
DR UniPathway; UPA00362; -.
DR Proteomes; UP000009136; 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 Acetylation; Branched-chain amino acid catabolism; Hydrolase;
KW Mitochondrion; Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 33..386
FT /note="3-hydroxyisobutyryl-CoA hydrolase, mitochondrial"
FT /id="PRO_0000284928"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 92
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q6NVY1"
FT MOD_RES 92
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 221
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 221
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NVY1"
FT MOD_RES 250
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 257
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 297
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 297
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 301
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 353
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 353
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NVY1"
FT MOD_RES 360
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 365
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 377
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
SQ SEQUENCE 386 AA; 43349 MW; 3920F7D82D6CBB09 CRC64;
MGLQGLCRLM SRFNSYKRTN IILQHLKMSN HTDAAAEVLL ERKGCAGVIT LNRPRFLNTL
TLGMIRQIYA QLKKWEQDPK TFLIIIKGAG EKAFCAGGDI RALSEARNTN QKMLQDLFRE
EYILNNAIDS CQKPYIALIH GITMGGGVGV SVHGQFRVAT EKSVFAMPET AIGLFPDVGG
GYFLPRLQGK LGYFLALTGF RLKGRDVYTA GIATHFVDFE KLGMLEEDLL ALKSPSKENI
ADVLETYHAK SKTDQDKPFI LEEHMDKINS WFSANTVEQI VDNLQQDGSS FALEQLKVIK
KMSPTSLKIT LRQLMEGSSK TLPEVLIMEY RLSQACMKGH DFHEGVRAVL IDKDQSPKWK
PADLKEVTDE DLNDYFKSLG SNDLKF
