ID   MCTE_CERS5              Reviewed;         285 AA.
AC   A4WNM9;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=Rsph17025_0082;
OS   Cereibacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=349102;
RN   [1] {ECO:0000312|EMBL:ABP68993.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17025 / ATH 2.4.3;
RG   US DOE Joint Genome Institute;
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   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M.,
RA   Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome of Rhodobacter sphaeroides ATCC 17025.";
RL   Submitted (APR-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; CP000661; ABP68993.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4WNM9; -.
DR   SMR; A4WNM9; -.
DR   STRING; 349102.Rsph17025_0082; -.
DR   EnsemblBacteria; ABP68993; ABP68993; Rsph17025_0082.
DR   KEGG; rsq:Rsph17025_0082; -.
DR   eggNOG; COG2301; Bacteria.
DR   HOGENOM; CLU_044864_0_1_5; -.
DR   OMA; WAMMETP; -.
DR   OrthoDB; 1107373at2; -.
DR   BioCyc; RSPH349102:G1G8M-81-MON; -.
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_0000405021"
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;  30777 MW;  CC9ED040612303FA CRC64;
     MAHQAHPFRS VLYIPGSKER ALEKAQGLAA DAIIFDLEDA VAHDEKIHAR DLLRKTLETA
     DYGRRIRIVR VNGMDTEWGR DDVAAFAGSK ADVILIPKVS SATDVQAVAD LIPDVPLWAM
     METALGMLNA AEIAAHPRLT GMVMGTNDLA KELTSRFRPD RLALQTGLGL CLLAARAHGL
     TIVDGVYNAF KDEDGLRAEC EHGRDMGFDG KTLIHPAQLE IANEVFSPSS AEIELANRQI
     AAFEEAERHG QGVAVVDGKI VENLHIVTAR QTLAKAEAIA AFGAS