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Protein

3-hydroxyisobutyryl-CoA hydrolase, mitochondrial

Gene

Hibch

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline catabolite. Has high activity toward isobutyryl-CoA. Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Also hydrolyzes 3-hydroxypropanoyl-CoA (By similarity).By similarity1 Publication

Catalytic activityi

3-hydroxy-2-methylpropanoyl-CoA + H2O = CoA + 3-hydroxy-2-methylpropanoate.1 Publication

Kineticsi

  1. KM=6 µM for 3-hydroxyisobutyryl-CoA1 Publication
  2. KM=25 µM for 3-hydroxypropionyl-CoA1 Publication
  1. Vmax=443 µmol/min/mg enzyme with 3-hydroxyisobutyryl-CoA as substrate1 Publication
  2. Vmax=250 µmol/min/mg enzyme with 3-hydroxypropionyl-CoA as substrate1 Publication

pH dependencei

Optimum pH is 7-9 with 3-hydroxyisobutyryl-CoA as substrate and 6 with 3-hydroxypropionyl-CoA as substrate.1 Publication

Pathwayi: L-valine degradation

This protein is involved in the pathway L-valine degradation, which is part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the pathway L-valine degradation and in Amino-acid degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei120 – 1201SubstrateBy similarity
Binding sitei145 – 1451Substrate; via amide nitrogenBy similarity
Binding sitei168 – 1681SubstrateBy similarity
Binding sitei176 – 1761SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Branched-chain amino acid catabolism

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-11699.
ReactomeiR-RNO-70895. Branched-chain amino acid catabolism.
SABIO-RKQ5XIE6.
UniPathwayiUPA00362.

Names & Taxonomyi

Protein namesi
Recommended name:
3-hydroxyisobutyryl-CoA hydrolase, mitochondrial (EC:3.1.2.4)
Alternative name(s):
3-hydroxyisobutyryl-coenzyme A hydrolase
Short name:
HIB-CoA hydrolase
Short name:
HIBYL-CoA-H
Gene namesi
Name:Hibch
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi1308392. Hibch.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3232Mitochondrion1 PublicationAdd
BLAST
Chaini33 – 3853533-hydroxyisobutyryl-CoA hydrolase, mitochondrialPRO_0000284931Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 541N6-acetyllysine; alternateBy similarity
Modified residuei54 – 541N6-succinyllysine; alternateBy similarity
Modified residuei91 – 911N6-acetyllysine; alternateBy similarity
Modified residuei91 – 911N6-succinyllysine; alternateBy similarity
Modified residuei100 – 1001N6-acetyllysine; alternateBy similarity
Modified residuei100 – 1001N6-succinyllysine; alternateBy similarity
Modified residuei220 – 2201N6-acetyllysine; alternateBy similarity
Modified residuei220 – 2201N6-succinyllysine; alternateBy similarity
Modified residuei249 – 2491N6-succinyllysineBy similarity
Modified residuei256 – 2561N6-succinyllysineBy similarity
Modified residuei296 – 2961N6-acetyllysine; alternateBy similarity
Modified residuei296 – 2961N6-succinyllysine; alternateBy similarity
Modified residuei300 – 3001N6-succinyllysineBy similarity
Modified residuei352 – 3521N6-acetyllysine; alternateBy similarity
Modified residuei352 – 3521N6-succinyllysine; alternateBy similarity
Modified residuei359 – 3591N6-acetyllysineBy similarity
Modified residuei364 – 3641N6-acetyllysineBy similarity
Modified residuei376 – 3761N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ5XIE6.
PRIDEiQ5XIE6.

PTM databases

iPTMnetiQ5XIE6.

Expressioni

Tissue specificityi

Highest activity in liver, kidney and heart. Low activity in muscle and brain.1 Publication

Gene expression databases

GenevisibleiQ5XIE6. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000032041.

Structurei

3D structure databases

ProteinModelPortaliQ5XIE6.
SMRiQ5XIE6. Positions 36-385.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1684. Eukaryota.
COG1024. LUCA.
GeneTreeiENSGT00570000079226.
HOGENOMiHOG000217005.
HOVERGENiHBG054809.
InParanoidiQ5XIE6.
KOiK05605.
OMAiIRMIYES.
OrthoDBiEOG7H1JKT.
PhylomeDBiQ5XIE6.
TreeFamiTF314329.

Family and domain databases

Gene3Di1.10.12.10. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR014748. Crontonase_C.
IPR032259. HIBYL-CoA-H.
[Graphical view]
PfamiPF16113. ECH_2. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5XIE6-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGQQFVWRLQ SRFSSIRRAS VILQHLRMSK HTETAEVLLE RRGCAGVITL
60 70 80 90 100
NRPKLLNALS LNMIRQIYPQ LKKWERDPDT FLIIIKGAGG KAFCAGGDIK
110 120 130 140 150
ALSEAKKAGQ TLSQDLFREE YILNNAIASC QKPYVALIDG ITMGGGVGLS
160 170 180 190 200
VHGQFRVATE RSLFAMPETG IGLFPDVGGG YFLPRLQGKL GYFLALTGFR
210 220 230 240 250
LKGRDVHRAG IATHFVDSEK LHVLEEELLA LKSPSAEDVA GVLESYHAKS
260 270 280 290 300
KMGQDKSIIF EEHMDKINSC FSANTVEQIL ENLRQDGSPF AMEQIKVINK
310 320 330 340 350
MSPTSLKITL RQLMEGSTKT LQEVLTMEYR LTQACMEGHD FHEGVRAVLI
360 370 380
DKDQTPKWKP ADLKDVTDED LNSYFKSLGS RDLKF
Length:385
Mass (Da):43,025
Last modified:May 1, 2007 - v2
Checksum:i1D9EB5AB4671DC6B
GO
Isoform 2 (identifier: Q5XIE6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     297-311: VINKMSPTSLKITLR → FSLTKTRLQNGNQLI
     312-385: Missing.

Note: No experimental confirmation available.
Show »
Length:311
Mass (Da):34,525
Checksum:i9B3DFF9AE465B863
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti344 – 3441G → V AA sequence (PubMed:8824301).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei297 – 31115VINKM…KITLR → FSLTKTRLQNGNQLI in isoform 2. 1 PublicationVSP_024781Add
BLAST
Alternative sequencei312 – 38574Missing in isoform 2. 1 PublicationVSP_024782Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03068835 Genomic DNA. No translation available.
AABR03067918 Genomic DNA. No translation available.
BC083737 mRNA. Translation: AAH83737.1.
RefSeqiNP_001013130.1. NM_001013112.1. [Q5XIE6-2]
XP_006244957.1. XM_006244895.1. [Q5XIE6-1]
UniGeneiRn.8745.

Genome annotation databases

EnsembliENSRNOT00000029677; ENSRNOP00000032041; ENSRNOG00000028557. [Q5XIE6-1]
ENSRNOT00000040650; ENSRNOP00000046370; ENSRNOG00000028557. [Q5XIE6-2]
GeneIDi301384.
KEGGirno:301384.
UCSCiRGD:1308392. rat. [Q5XIE6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03068835 Genomic DNA. No translation available.
AABR03067918 Genomic DNA. No translation available.
BC083737 mRNA. Translation: AAH83737.1.
RefSeqiNP_001013130.1. NM_001013112.1. [Q5XIE6-2]
XP_006244957.1. XM_006244895.1. [Q5XIE6-1]
UniGeneiRn.8745.

3D structure databases

ProteinModelPortaliQ5XIE6.
SMRiQ5XIE6. Positions 36-385.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000032041.

PTM databases

iPTMnetiQ5XIE6.

Proteomic databases

PaxDbiQ5XIE6.
PRIDEiQ5XIE6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000029677; ENSRNOP00000032041; ENSRNOG00000028557. [Q5XIE6-1]
ENSRNOT00000040650; ENSRNOP00000046370; ENSRNOG00000028557. [Q5XIE6-2]
GeneIDi301384.
KEGGirno:301384.
UCSCiRGD:1308392. rat. [Q5XIE6-1]

Organism-specific databases

CTDi26275.
RGDi1308392. Hibch.

Phylogenomic databases

eggNOGiKOG1684. Eukaryota.
COG1024. LUCA.
GeneTreeiENSGT00570000079226.
HOGENOMiHOG000217005.
HOVERGENiHBG054809.
InParanoidiQ5XIE6.
KOiK05605.
OMAiIRMIYES.
OrthoDBiEOG7H1JKT.
PhylomeDBiQ5XIE6.
TreeFamiTF314329.

Enzyme and pathway databases

UniPathwayiUPA00362.
BioCyciMetaCyc:MONOMER-11699.
ReactomeiR-RNO-70895. Branched-chain amino acid catabolism.
SABIO-RKQ5XIE6.

Miscellaneous databases

PROiQ5XIE6.

Gene expression databases

GenevisibleiQ5XIE6. RN.

Family and domain databases

Gene3Di1.10.12.10. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR014748. Crontonase_C.
IPR032259. HIBYL-CoA-H.
[Graphical view]
PfamiPF16113. ECH_2. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Heart.
  3. "Primary structure and tissue-specific expression of human beta-hydroxyisobutyryl-coenzyme A hydrolase."
    Hawes J.W., Jaskiewicz J., Shimomura Y., Huang B., Bunting J., Harper E.T., Harris R.A.
    J. Biol. Chem. 271:26430-26434(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 33-43; 45-56; 167-184; 209-221 AND 337-344, SUBCELLULAR LOCATION.
    Tissue: Brain.
  4. "Purification and partial characterization of 3-hydroxyisobutyryl-coenzyme A hydrolase of rat liver."
    Shimomura Y., Murakami T., Fujitsuka N., Nakai N., Sato Y., Sugiyama S., Shimomura N., Irwin J., Hawes J.W., Harris R.A.
    J. Biol. Chem. 269:14248-14253(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.

Entry informationi

Entry nameiHIBCH_RAT
AccessioniPrimary (citable) accession number: Q5XIE6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2007
Last modified: June 8, 2016
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.