ID S9W861_SCHCR Unreviewed; 428 AA.
AC S9W861;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=3-hydroxyisobutyryl-CoA hydrolase {ECO:0000256|ARBA:ARBA00011915};
DE EC=3.1.2.4 {ECO:0000256|ARBA:ARBA00011915};
GN ORFNames=SPOG_02843 {ECO:0000313|EMBL:EPY53935.1};
OS Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 /
OS NBRC 106824 / NRRL Y48691) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY53935.1, ECO:0000313|Proteomes:UP000015464};
RN [1] {ECO:0000313|EMBL:EPY53935.1, ECO:0000313|Proteomes:UP000015464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC {ECO:0000313|Proteomes:UP000015464};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
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};
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DR EMBL; KE546988; EPY53935.1; -; Genomic_DNA.
DR RefSeq; XP_013020958.1; XM_013165504.1.
DR AlphaFoldDB; S9W861; -.
DR STRING; 653667.S9W861; -.
DR EnsemblFungi; EPY53935; EPY53935; SPOG_02843.
DR GeneID; 25037164; -.
DR eggNOG; KOG1684; Eukaryota.
DR HOGENOM; CLU_009834_22_1_1; -.
DR OMA; LVWEQIR; -.
DR OrthoDB; 3639304at2759; -.
DR Proteomes; UP000015464; Unassembled WGS sequence.
DR GO; GO:0003860; F:3-hydroxyisobutyryl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR CDD; cd06558; crotonase-like; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR045004; ECH_dom.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
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.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EPY53935.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015464}.
FT DOMAIN 65..384
FT /note="Enoyl-CoA hydratase/isomerase"
FT /evidence="ECO:0000259|Pfam:PF16113"
SQ SEQUENCE 428 AA; 48159 MW; 37E556510E2441A5 CRC64;
MNGRNLTVKG SSILHFCKRN YLPLDSLSNR FSMSRARILN QKFKSTLASN SSSGSILMEK
KLGARVLTLN RPEKLNALNL EMIDSLHSKL VKLEQSELAK VIVLQGKGRA FSSGGDVKDA
AGRIKQGELS NVRKAFTEEY RLCHTIATYK KPVVAFMNGI TMGGGAGLTM HAPFRIACED
TKFAMPETTI GYFTDVGSSF FFNRMPSHVG KFLALTSNVV SGEDCVPLGI ATHYVPKHMF
EELENRLADL NTSDLHMIND TISEFCGECP QPSSLLNVEN LRLIDSCFGM RDPVRIIRAL
EEQVQSNSDV PDFAKQTLET LLKKSPLSLA VTNSLIERAG MWTISEALMY DQIVSYHMLN
QPDFIIGVDA QLISKTRNPK WSYSWDHQFG DLEQVYKVPE EYKNGIQYHS KDRSHSRLWD
YNAYPYRA
//
