ID B0CSR7_LACBS Unreviewed; 493 AA.
AC B0CSR7;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=3-hydroxyisobutyryl-CoA hydrolase {ECO:0000256|ARBA:ARBA00011915};
DE EC=3.1.2.4 {ECO:0000256|ARBA:ARBA00011915};
GN ORFNames=LACBIDRAFT_292320 {ECO:0000313|EMBL:EDR14353.1};
OS Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS (Laccaria laccata var. bicolor).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=486041 {ECO:0000313|Proteomes:UP000001194};
RN [1] {ECO:0000313|EMBL:EDR14353.1, ECO:0000313|Proteomes:UP000001194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 / ATCC MYA-4686 {ECO:0000313|Proteomes:UP000001194};
RX PubMed=18322534; DOI=10.1038/nature06556;
RA Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA Tuskan G., Grigoriev I.V.;
RT "The genome of Laccaria bicolor provides insights into mycorrhizal
RT symbiosis.";
RL Nature 452:88-92(2008).
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; DS547092; EDR14353.1; -; Genomic_DNA.
DR RefSeq; XP_001874912.1; XM_001874877.1.
DR AlphaFoldDB; B0CSR7; -.
DR STRING; 486041.B0CSR7; -.
DR GeneID; 6070852; -.
DR KEGG; lbc:LACBIDRAFT_292320; -.
DR HOGENOM; CLU_009834_22_0_1; -.
DR InParanoid; B0CSR7; -.
DR OrthoDB; 3639304at2759; -.
DR Proteomes; UP000001194; 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; 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.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EDR14353.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001194}.
FT DOMAIN 52..391
FT /note="Enoyl-CoA hydratase/isomerase"
FT /evidence="ECO:0000259|Pfam:PF16113"
SQ SEQUENCE 493 AA; 54290 MW; 39A7116D11AE50DB CRC64;
MPTTAIFRSM TCGAVRTASH RAKAIGHHMM STTTSSTSEP TVKFESNSAL RSYILDRPLK
RNALDEQMLT LLRPKIEEWS ASDLCGTIVG RGSGPVFCSG GDVASVVQNA ADPATRPKAM
DFFKREFEMD YILAALKKPY VVIMDGVTMG GGVGLAAPAP FRVATENTQF AMPEAKIGYF
PDVGGSYFLS RLDGEIGTYL ALTSQTLKGR AVFEYGFATH FIPSRRIPML LDRLAELDQP
HPSLVDHTLE ELSSERDDSE PPALFTGRLR VALDSAFRHD SVERIFKDLR TLLQDGDATV
RQWASDSLEM LAMRSPTSLK VALKAIRRGK RMTLREALEM ELKIASAYCS GASPDFDIGV
KAVLIEKLKT RPEWSPSSLE GVSEDIVSRF FEPTSPYVSS APRLEIPEHL AAEAISIPMR
YALPSENEIG AVIRGSHSSG GEMGTRAEDV LARFAELRPG KLGVKEKVLE VIQRRCKVTD
NADGNFVWLK WIH
//
