ID G7CC99_MYCT3 Unreviewed; 350 AA. AC G7CC99; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAR-2024, entry version 56. DE RecName: Full=3-hydroxyisobutyryl-CoA hydrolase {ECO:0000256|ARBA:ARBA00011915}; DE EC=3.1.2.4 {ECO:0000256|ARBA:ARBA00011915}; GN ORFNames=KEK_02971 {ECO:0000313|EMBL:EHI14362.1}; OS Mycolicibacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP OS 105390 / JCM 6362 / NCTC 10409 / 316) (Mycobacterium thermoresistibile). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycolicibacterium. OX NCBI_TaxID=1078020 {ECO:0000313|EMBL:EHI14362.1, ECO:0000313|Proteomes:UP000004915}; RN [1] {ECO:0000313|EMBL:EHI14362.1, ECO:0000313|Proteomes:UP000004915} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 / RC 316 {ECO:0000313|Proteomes:UP000004915}; RG Tuberculosis Structural Genomics Consortium; RA Ioerger T.R.; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0007829|PDB:4HDT} RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-350 IN COMPLEX WITH ZINC. RX PubMed=25613812; DOI=10.1016/j.tube.2014.12.003; RA Baugh L., Phan I., Begley D.W., Clifton M.C., Armour B., Dranow D.M., RA Taylor B.M., Muruthi M.M., Abendroth J., Fairman J.W., Fox D., RA Dieterich S.H., Staker B.L., Gardberg A.S., Choi R., Hewitt S.N., RA Napuli A.J., Myers J., Barrett L.K., Zhang Y., Ferrell M., Mundt E., RA Thompkins K., Tran N., Lyons-Abbott S., Abramov A., Sekar A., RA Serbzhinskiy D., Lorimer D., Buchko G.W., Stacy R., Stewart L.J., RA Edwards T.E., Van Voorhis W.C., Myler P.J.; RT "Increasing the structural coverage of tuberculosis drug targets."; RL Tuberculosis 95:142-148(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}; CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EHI14362.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AGVE01000017; EHI14362.1; -; Genomic_DNA. DR RefSeq; WP_003924040.1; NZ_AGVE01000017.1. DR PDB; 4HDT; X-ray; 1.60 A; A=2-350. DR PDBsum; 4HDT; -. DR AlphaFoldDB; G7CC99; -. DR SMR; G7CC99; -. DR PATRIC; fig|1078020.3.peg.585; -. DR eggNOG; COG1024; Bacteria. DR Proteomes; UP000004915; Unassembled WGS sequence. DR GO; GO:0003860; F:3-hydroxyisobutyryl-CoA hydrolase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:4HDT}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EHI14362.1}; KW Metal-binding {ECO:0007829|PDB:4HDT}; KW Reference proteome {ECO:0000313|Proteomes:UP000004915}; KW Zinc {ECO:0007829|PDB:4HDT}. FT DOMAIN 16..336 FT /note="Enoyl-CoA hydratase/isomerase" FT /evidence="ECO:0000259|Pfam:PF16113" FT BINDING 32 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4HDT" FT BINDING 46 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4HDT" FT BINDING 61 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:4HDT" FT BINDING 75 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0007829|PDB:4HDT" FT BINDING 83 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4HDT" FT BINDING 97 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4HDT" FT BINDING 189 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:4HDT" FT BINDING 193 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0007829|PDB:4HDT" FT BINDING 348 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4HDT" SQ SEQUENCE 350 AA; 37240 MW; 03FF93D19FE338E6 CRC64; MTAKNEDVLV NVEGGVGLLT LNRPKAINSL THGMVTTMAE RLAAWENDDS VRAVLLTGAG ERGLCAGGDV VAIYHSAKAD GAEARRFWFD EYRLNAHIGR YPKPYVSIMD GIVMGGGVGV GAHGNVRVVT DTTKMAMPEV GIGFIPDVGG TYLLSRAPGK LGLHAALTGA PFSGADAIVM GFADHYVPHD KIDEFTRAVI ADGVDAALAA HAQEPPASPL AEQRSWIDEC YTGDTVADII AALRAHDAPA AGEAADLIAT RSPIALSVTL ESVRRAAKLQ SLEDTLRQEY RVSCASLKSH DLVEGIRAQL VDKDRNPKWR PATLAEVTEA DVEAYFAPVD PELTFEGETQ //