ID   MCTE_CERSK              Reviewed;         285 AA.
AC   B9KNB6;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=RSKD131_2362;
OS   Cereibacter sphaeroides (strain KD131 / KCTC 12085) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=557760;
RN   [1] {ECO:0000312|EMBL:ACM02222.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KD131 / KCTC 12085;
RX   PubMed=19028901; DOI=10.1128/jb.01565-08;
RA   Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.;
RT   "Complete genome sequence of Rhodobacter sphaeroides KD131.";
RL   J. Bacteriol. 191:1118-1119(2009).
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; CP001150; ACM02222.1; -; Genomic_DNA.
DR   RefSeq; WP_015921374.1; NC_011963.1.
DR   AlphaFoldDB; B9KNB6; -.
DR   SMR; B9KNB6; -.
DR   EnsemblBacteria; ACM02222; ACM02222; RSKD131_2362.
DR   GeneID; 67447741; -.
DR   KEGG; rsk:RSKD131_2362; -.
DR   HOGENOM; CLU_044864_0_1_5; -.
DR   OMA; WAMMETP; -.
DR   Proteomes; UP000001597; Chromosome 1.
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_0000405022"
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;  30931 MW;  381CDA1380B75CBA CRC64;
     MAHQAHPFRS VLYIPGSKER ALEKARGLAA DAIIFDLEDA VAHDEKIHAR RLLKTTLETA
     DYGHRFRIVR VNGMDTEWGR ADLEAFAEAK ADAILIPKVS RAADLEAVAA LVPDLPLWAM
     METAQGMLNA AEIAAHPRLT GMVMGTNDLA KELGSRYRPD RLAMQAGLGL CLLAARAHGL
     TIVDGVYNAF RDEEGLRAEC EQGRDMGFDG KTLIHPAQLE IANAVFSPSP AEIELANRQI
     AAFEEAERHG QGVAVVDGKI VENLHIVTAR QTLAKAEAIA AFRAS