ID   MCAL_CERS1              Reviewed;         318 AA.
AC   A3PGR7;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=L-malyl-CoA/beta-methylmalyl-CoA lyase {ECO:0000250|UniProtKB:Q3J5L6};
DE            EC=4.1.3.24;
DE   AltName: Full=(3S)-malyl-CoA/beta-methylmalyl-CoA lyase {ECO:0000250|UniProtKB:Q3J5L6};
GN   Name=mcl1 {ECO:0000250|UniProtKB:Q3J5L6}; OrderedLocusNames=Rsph17029_0417;
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:ABN75533.1}
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: Involved in the ethylmalonyl-CoA pathway for acetate
CC       assimilation. Catalyzes the reversible condensation of glyoxylate and
CC       acetyl-CoA to L-malyl-CoA and the reversible condensation of glyoxylate
CC       and propionyl-CoA to yield beta-methylmalyl-CoA (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malyl-CoA = acetyl-CoA + glyoxylate; Xref=Rhea:RHEA:16629,
CC         ChEBI:CHEBI:36655, ChEBI:CHEBI:57288, ChEBI:CHEBI:57317; EC=4.1.3.24;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-beta-methylmalyl-CoA = glyoxylate + propanoyl-CoA;
CC         Xref=Rhea:RHEA:38259, ChEBI:CHEBI:36655, ChEBI:CHEBI:57392,
CC         ChEBI:CHEBI:75634; EC=4.1.3.24;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Divalent cations such as magnesium or manganese. {ECO:0000250};
CC   -!- SUBUNIT: Homohexamer. Dimer of trimers (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family. {ECO:0000305}.
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DR   EMBL; CP000577; ABN75533.1; -; Genomic_DNA.
DR   RefSeq; WP_011336971.1; NC_009049.1.
DR   AlphaFoldDB; A3PGR7; -.
DR   SMR; A3PGR7; -.
DR   EnsemblBacteria; ABN75533; ABN75533; Rsph17029_0417.
DR   GeneID; 57469111; -.
DR   KEGG; rsh:Rsph17029_0417; -.
DR   HOGENOM; CLU_044864_0_1_5; -.
DR   OMA; WDIHYLD; -.
DR   GO; GO:0043959; F:L-erythro-3-methylmalyl-CoA lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050083; F:malyl-CoA lyase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
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   Lyase; Magnesium; Manganese; Metal-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:B6E2X2"
FT   CHAIN           2..318
FT                   /note="L-malyl-CoA/beta-methylmalyl-CoA lyase"
FT                   /id="PRO_0000404703"
FT   BINDING         19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         24
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         30
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9RUZ0"
FT   BINDING         141
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         167..168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         251..252
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   318 AA;  34288 MW;  E366B25B7A193AC1 CRC64;
     MSFRLQPAPP ARPNRCQLFG PGSRPALFEK MAASAADVIN LDLEDSVAPD DKAQARANII
     EAINGLDWGR KYLSVRINGL DTPFWYRDVV DLLEQAGDRL DQIMIPKVGC AADVYAVDAL
     VTAIERAKGR TKPLSFEVII ESAAGIAHVE EIAASSPRLQ AMSLGAADFA ASMGMQTTGI
     GGTQENYYML HDGQKHWSDP WHWAQAAIVA ACRTHGILPV DGPFGDFSDD EGFRAQARRS
     ATLGMVGKWA IHPKQVALAN EVFTPSETAV TEAREILAAM DAAKARGEGA TVYKGRLVDI
     ASIKQAEVIV RQAEMISA