HIBCH_RAT
ID HIBCH_RAT Reviewed; 385 AA.
AC Q5XIE6;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 118.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 33-43; 45-56; 167-184; 209-221 AND 337-344, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=8824301; DOI=10.1074/jbc.271.42.26430;
RA Hawes J.W., Jaskiewicz J., Shimomura Y., Huang B., Bunting J., Harper E.T.,
RA Harris R.A.;
RT "Primary structure and tissue-specific expression of human beta-
RT hydroxyisobutyryl-coenzyme A hydrolase.";
RL J. Biol. Chem. 271:26430-26434(1996).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=8188708; DOI=10.1016/s0021-9258(17)36781-9;
RA Shimomura Y., Murakami T., Fujitsuka N., Nakai N., Sato Y., Sugiyama S.,
RA Shimomura N., Irwin J., Hawes J.W., Harris R.A.;
RT "Purification and partial characterization of 3-hydroxyisobutyryl-coenzyme
RT A hydrolase of rat liver.";
RL J. Biol. Chem. 269:14248-14253(1994).
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 ECO:0000269|PubMed:8188708}.
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:0000269|PubMed:8188708};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6 uM for 3-hydroxyisobutyryl-CoA {ECO:0000269|PubMed:8188708};
CC KM=25 uM for 3-hydroxypropionyl-CoA {ECO:0000269|PubMed:8188708};
CC Vmax=443 umol/min/mg enzyme with 3-hydroxyisobutyryl-CoA as substrate
CC {ECO:0000269|PubMed:8188708};
CC Vmax=250 umol/min/mg enzyme with 3-hydroxypropionyl-CoA as substrate
CC {ECO:0000269|PubMed:8188708};
CC pH dependence:
CC Optimum pH is 7-9 with 3-hydroxyisobutyryl-CoA as substrate and 6
CC with 3-hydroxypropionyl-CoA as substrate.
CC {ECO:0000269|PubMed:8188708};
CC -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:8824301}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5XIE6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5XIE6-2; Sequence=VSP_024781, VSP_024782;
CC -!- TISSUE SPECIFICITY: Highest activity in liver, kidney and heart. Low
CC activity in muscle and brain. {ECO:0000269|PubMed:8188708}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
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DR EMBL; AABR03068835; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03067918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC083737; AAH83737.1; -; mRNA.
DR RefSeq; NP_001013130.1; NM_001013112.1. [Q5XIE6-2]
DR RefSeq; XP_006244957.1; XM_006244895.1. [Q5XIE6-1]
DR AlphaFoldDB; Q5XIE6; -.
DR SMR; Q5XIE6; -.
DR STRING; 10116.ENSRNOP00000032041; -.
DR iPTMnet; Q5XIE6; -.
DR PhosphoSitePlus; Q5XIE6; -.
DR jPOST; Q5XIE6; -.
DR PaxDb; Q5XIE6; -.
DR PRIDE; Q5XIE6; -.
DR Ensembl; ENSRNOT00000029677; ENSRNOP00000032041; ENSRNOG00000028557. [Q5XIE6-1]
DR Ensembl; ENSRNOT00000040650; ENSRNOP00000046370; ENSRNOG00000028557. [Q5XIE6-2]
DR GeneID; 301384; -.
DR KEGG; rno:301384; -.
DR UCSC; RGD:1308392; rat. [Q5XIE6-1]
DR CTD; 26275; -.
DR RGD; 1308392; Hibch.
DR eggNOG; KOG1684; Eukaryota.
DR GeneTree; ENSGT00890000139491; -.
DR HOGENOM; CLU_009834_22_2_1; -.
DR InParanoid; Q5XIE6; -.
DR OMA; GKPYIAF; -.
DR OrthoDB; 1369862at2759; -.
DR PhylomeDB; Q5XIE6; -.
DR TreeFam; TF314329; -.
DR BioCyc; MetaCyc:MON-11699; -.
DR Reactome; R-RNO-70895; Branched-chain amino acid catabolism.
DR SABIO-RK; Q5XIE6; -.
DR UniPathway; UPA00362; -.
DR PRO; PR:Q5XIE6; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000028557; Expressed in heart and 20 other tissues.
DR Genevisible; Q5XIE6; RN.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0003860; F:3-hydroxyisobutyryl-CoA hydrolase activity; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Branched-chain amino acid catabolism;
KW Direct protein sequencing; Hydrolase; Mitochondrion; Phosphoprotein;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:8824301"
FT CHAIN 33..385
FT /note="3-hydroxyisobutyryl-CoA hydrolase, mitochondrial"
FT /id="PRO_0000284931"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 54
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 54
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 91
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q6NVY1"
FT MOD_RES 91
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 100
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 100
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 220
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 220
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NVY1"
FT MOD_RES 249
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 256
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 296
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 296
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 300
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 352
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 352
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 359
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 364
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 376
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT VAR_SEQ 297..311
FT /note="VINKMSPTSLKITLR -> FSLTKTRLQNGNQLI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024781"
FT VAR_SEQ 312..385
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024782"
FT CONFLICT 344
FT /note="G -> V (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 43025 MW; 1D9EB5AB4671DC6B CRC64;
MGQQFVWRLQ SRFSSIRRAS VILQHLRMSK HTETAEVLLE RRGCAGVITL NRPKLLNALS
LNMIRQIYPQ LKKWERDPDT FLIIIKGAGG KAFCAGGDIK ALSEAKKAGQ TLSQDLFREE
YILNNAIASC QKPYVALIDG ITMGGGVGLS VHGQFRVATE RSLFAMPETG IGLFPDVGGG
YFLPRLQGKL GYFLALTGFR LKGRDVHRAG IATHFVDSEK LHVLEEELLA LKSPSAEDVA
GVLESYHAKS KMGQDKSIIF EEHMDKINSC FSANTVEQIL ENLRQDGSPF AMEQIKVINK
MSPTSLKITL RQLMEGSTKT LQEVLTMEYR LTQACMEGHD FHEGVRAVLI DKDQTPKWKP
ADLKDVTDED LNSYFKSLGS RDLKF
