MCTE_CERS4
ID MCTE_CERS4 Reviewed; 285 AA.
AC D3JV05; Q3IZ81;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=(3S)-malyl-CoA thioesterase {ECO:0000312|EMBL:ADC44454.1};
DE EC=3.1.2.30;
DE AltName: Full=(3S)-malyl-CoA thiolesterase;
GN Name=mcl2 {ECO:0000312|EMBL:ADC44454.1}; OrderedLocusNames=RHOS4_25850;
GN ORFNames=RSP_0970;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ADC44454.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND INDUCTION.
RX PubMed=20047909; DOI=10.1128/jb.01267-09;
RA Erb T.J., Frerichs-Revermann L., Fuchs G., Alber B.E.;
RT "The apparent malate synthase activity of Rhodobacter sphaeroides is due to
RT two paralogous enzymes, (3S)-Malyl-coenzyme A (CoA)/{beta}-methylmalyl-CoA
RT lyase and (3S)- Malyl-CoA thioesterase.";
RL J. Bacteriol. 192:1249-1258(2010).
RN [2] {ECO:0000312|EMBL:ABA80153.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) 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 {ECO:0000269|PubMed:20047909}.
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 Evidence={ECO:0000269|PubMed:20047909};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:20047909};
CC -!- ACTIVITY REGULATION: Reversibly inhibited by EDTA. Stimulated by the
CC divalent cations Mg(2+) and Mn(2+). {ECO:0000269|PubMed:20047909}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.09 mM for (3S)-malyl-CoA (in the presence of Mg(2+) or Mn(2+))
CC {ECO:0000269|PubMed:20047909};
CC -!- SUBUNIT: Homodimer or homotrimer. {ECO:0000269|PubMed:20047909}.
CC -!- INDUCTION: Induced by growth on acetate. {ECO:0000269|PubMed:20047909}.
CC -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family. {ECO:0000305}.
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DR EMBL; GU320613; ADC44454.1; -; Genomic_DNA.
DR EMBL; CP000143; ABA80153.1; -; Genomic_DNA.
DR RefSeq; WP_011338634.1; NZ_CP030271.1.
DR RefSeq; YP_354054.1; NC_007493.2.
DR AlphaFoldDB; D3JV05; -.
DR SMR; D3JV05; -.
DR STRING; 272943.RSP_0970; -.
DR EnsemblBacteria; ABA80153; ABA80153; RSP_0970.
DR KEGG; rsp:RSP_0970; -.
DR PATRIC; fig|272943.9.peg.2942; -.
DR eggNOG; COG2301; Bacteria.
DR OMA; WAMMETP; -.
DR PhylomeDB; D3JV05; -.
DR BRENDA; 3.1.2.30; 5383.
DR SABIO-RK; D3JV05; -.
DR Proteomes; UP000002703; 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 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..285
FT /note="(3S)-malyl-CoA thioesterase"
FT /id="PRO_0000405020"
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; 30861 MW; 3CBBCE1769474437 CRC64;
MAHQAHPFRS VLYIPGSKER ALEKAQGLAA DAIIFDLEDA VAHDEKIHAR RLLKTTLETA
DYGHRFRIVR VNGMDTEWGR ADLEAFAEAK ADAILIPKVS RAADLEAVAA LVPDLPLWAM
METAQGMLNA AEIAAHPRLS GMVMGTNDLA KELGSRYRPD RLAMQAGLGL CLLAARAHGL
TIVDGVYNAF KDEEGLRAEC EQGRDMGFDG KTLIHPAQLE IANAVFSPSP AEIELANRQI
AAFEEAERHG QGVAVVDGKI VENLHIVTAR QTLAKAEAIA AFRAS
