(data stored in SCRATCH zone)

SWISSPROT: Q750D1_ASHGO

ID   Q750D1_ASHGO            Unreviewed;       477 AA.
AC   Q750D1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 93.
DE   RecName: Full=3-hydroxyisobutyryl-CoA hydrolase, mitochondrial {ECO:0000256|RuleBase:RU363052};
DE            EC=3.1.2.4 {ECO:0000256|RuleBase:RU363052};
DE   AltName: Full=3-hydroxyisobutyryl-coenzyme A hydrolase {ECO:0000256|RuleBase:RU363052};
GN   ORFNames=AGOS_AGR024C {ECO:0000313|EMBL:AAS54513.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS54513.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54513.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline
CC       catabolite. {ECO:0000256|RuleBase:RU363052}.
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|RuleBase:RU363052};
CC   -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC       {ECO:0000256|RuleBase:RU363052}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|RuleBase:RU363052}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000256|RuleBase:RU363052}.
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DR   EMBL; AE016820; AAS54513.1; -; Genomic_DNA.
DR   RefSeq; NP_986689.1; NM_211751.1.
DR   STRING; 33169.AAS54513; -.
DR   EnsemblFungi; AAS54513; AAS54513; AGOS_AGR024C.
DR   GeneID; 4622988; -.
DR   KEGG; ago:AGOS_AGR024C; -.
DR   HOGENOM; HOG000217005; -.
DR   InParanoid; Q750D1; -.
DR   KO; K05605; -.
DR   OMA; LNRMPGK; -.
DR   UniPathway; UPA00362; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005763; C:mitochondrial small ribosomal subunit; IEA:EnsemblFungi.
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:0003735; F:structural constituent of ribosome; IEA:EnsemblFungi.
DR   GO; GO:0006574; P:valine catabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR032259; HIBYL-CoA-H.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   Pfam; PF16113; ECH_2; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   PROSITE; PS50096; IQ; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q750D1.
DR   SWISS-2DPAGE; Q750D1.
KW   Branched-chain amino acid catabolism {ECO:0000256|RuleBase:RU363052};
KW   Hydrolase {ECO:0000256|RuleBase:RU363052};
KW   Mitochondrion {ECO:0000256|RuleBase:RU363052};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Transit peptide {ECO:0000256|RuleBase:RU363052}.
SQ   SEQUENCE   477 AA;  53636 MW;  3B3650377E9C2E6B CRC64;
     MIRSTVRGMV QRRQMSSLVK FKTNNTARVV TLNRPEKLNA INHEICHSIL PVMQEYAKSD
     VANVIVFDSA CAPRAFCAGG DIVLMAKAMR RDMLEKVDDF FQGEYTMNWM LATYPKPVVA
     LMDGITMGGG VGLTIHVPFR VATENTKWAM PELDIGLHPD VGVSFALPRI MTLGGQEGQL
     GYYLCLTGEV LQGADVYMAG LASHYVESTQ HGALKERLGT VPITRKADET FANTNAVIEE
     FSSPLPDGYQ FKYNKEELDV IERFFHYDVS YKELRKNLEA FASSNANSEV ARNFAKATLE
     KLSTKSTVSA EITREQFRRN SQRDIQSAMK QDLITSTNLL RNNELAEFEN AVIHKLVEKA
     KTPYEWKNTS PSVADISKLL AADPANPIDL LETFGVTFKN YRYHNKFTLP TEAAVQAYIT
     GTDQSGRSMA VTRAETVKYF TEFNPVSRGK VGTEYVVNLI IDRKCRMDND SFLHWNY
//

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