MCTE_CERS1
ID MCTE_CERS1 Reviewed; 285 AA.
AC A3PN16;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=(3S)-malyl-CoA thioesterase {ECO:0000250|UniProtKB:D3JV05};
DE EC=3.1.2.30;
DE AltName: Full=(3S)-malyl-CoA thiolesterase {ECO:0000250|UniProtKB:D3JV05};
GN Name=mcl2 {ECO:0000250|UniProtKB:D3JV05}; OrderedLocusNames=Rsph17029_2630;
OS Cereibacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=349101;
RN [1] {ECO:0000312|EMBL:ABN77732.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17029 / ATH 2.4.9;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.,
RA Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides ATCC 17029.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolysis of (3S)-malyl-CoA to (3S)-malate and
CC free CoA. Inactive towards beta-methylmalyl-CoA and other CoA esters
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malyl-CoA + H2O = (S)-malate + CoA + H(+);
CC Xref=Rhea:RHEA:38291, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15589, ChEBI:CHEBI:57287, ChEBI:CHEBI:57317; EC=3.1.2.30;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:D3JV05};
CC -!- SUBUNIT: Homodimer or homotrimer. {ECO:0000250|UniProtKB:D3JV05}.
CC -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family. {ECO:0000305}.
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DR EMBL; CP000577; ABN77732.1; -; Genomic_DNA.
DR RefSeq; WP_011841795.1; NC_009049.1.
DR AlphaFoldDB; A3PN16; -.
DR SMR; A3PN16; -.
DR EnsemblBacteria; ABN77732; ABN77732; Rsph17029_2630.
DR GeneID; 57471301; -.
DR KEGG; rsh:Rsph17029_2630; -.
DR HOGENOM; CLU_044864_0_1_5; -.
DR OMA; WAMMETP; -.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.60; -; 1.
DR InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR InterPro; IPR011206; Citrate_lyase_beta/mcl1/mcl2.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR Pfam; PF03328; HpcH_HpaI; 1.
DR PIRSF; PIRSF015582; Cit_lyase_B; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding.
FT CHAIN 1..285
FT /note="(3S)-malyl-CoA thioesterase"
FT /id="PRO_0000405019"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9RUZ0"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9RUZ0"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9RUZ0"
FT BINDING 148
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9RUZ0"
SQ SEQUENCE 285 AA; 30818 MW; F1BCB61B24012D9D CRC64;
MAHQAHPFRS VLYIPGSKER ALEKAQGLAA DAIIFDLEDA VAHDEKIHAR ALLKTTLETV
DYGHRFRIVR VNGMDTEWGR ADLEAFAEAK ADAILIPKVS RAADLEAVAA LVPDLPLWAM
METAQGMLNA AEIAAHPRLT GMVMGTNDLA KELGSRYRPD RLAMQAGLGL CLLAARAHGL
TIVDGVYNAF KDEEGLRAEC EQGRDMGFDG KTLIHPAQLE IANAVFSPSP AEIELANRQI
AAFEEAERHG QGVAVVDGKI VENLHIVTAR QTLAKAEAIA AFRAS
