ID B8LSS2_TALSN Unreviewed; 495 AA.
AC B8LSS2;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=3-hydroxyisobutyryl-CoA hydrolase {ECO:0000256|ARBA:ARBA00011915};
DE EC=3.1.2.4 {ECO:0000256|ARBA:ARBA00011915};
GN ORFNames=TSTA_063930 {ECO:0000313|EMBL:EED22918.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED22918.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; EQ962652; EED22918.1; -; Genomic_DNA.
DR RefSeq; XP_002340305.1; XM_002340264.1.
DR AlphaFoldDB; B8LSS2; -.
DR STRING; 441959.B8LSS2; -.
DR GeneID; 8108617; -.
DR VEuPathDB; FungiDB:TSTA_063930; -.
DR eggNOG; KOG1684; Eukaryota.
DR HOGENOM; CLU_009834_22_0_1; -.
DR InParanoid; B8LSS2; -.
DR OMA; EWEKSDM; -.
DR OrthoDB; 3639304at2759; -.
DR PhylomeDB; B8LSS2; -.
DR Proteomes; UP000001745; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EED22918.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745}.
FT DOMAIN 66..409
FT /note="Enoyl-CoA hydratase/isomerase"
FT /evidence="ECO:0000259|Pfam:PF16113"
FT COILED 307..334
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 495 AA; 55507 MW; 9A42C5516F0DF5DF CRC64;
MLLRPTFHRA STPLSRLSRS SFAAMPLRAK VTNPAFASKM SLSTKSSENP AVDSDDVLFY
STYGLRLIEL NRPKKLNSLN GSMCQQIIPR LLEWEKSQLA NIIMVSGRGE KALCAGGDVA
ALAINNKEGP EGVKRSQDYF ALEYQLDHLI ATYSKPFVAV MDGITMGGGV GLSVHAPFRI
ATERTLFAMP ETTIGFFPDV GGSFFLSRLD GEVGTYLALT SERLNGVQAF YTGIATHYVD
SSVLSNLTNR LAELVFKDYA NLNERNDLVN KTIAEFSTGL PSVEKEPILL RYKLRQAIDR
CFKYNTVEEI IQALEKEEDQ KEWARKTLET LTSRSPTSLK VTLRQLRLGK NWSIKETFQR
EHAIASVFMN HPDFVEGVSA RLISKPPRTP EWNPSRLEDV TPADVDAFFK IDGEPLPTFH
DNDYKTYPHA KYALPTEADI EAFVRGNKTT GSDTVKEFVQ NWGQKEGVRA KVTEVLGRRT
KKTDKGLEWI ETDKE
//
