ID   MCAL_CERS5              Reviewed;         318 AA.
AC   A4WVF5;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 2.
DT   03-AUG-2022, entry version 78.
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=Rsph17025_2481;
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:ABP71369.1}
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: 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABP71369.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000661; ABP71369.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A4WVF5; -.
DR   SMR; A4WVF5; -.
DR   STRING; 349102.Rsph17025_2481; -.
DR   PRIDE; A4WVF5; -.
DR   EnsemblBacteria; ABP71369; ABP71369; Rsph17025_2481.
DR   KEGG; rsq:Rsph17025_2481; -.
DR   eggNOG; COG2301; Bacteria.
DR   HOGENOM; CLU_044864_0_1_5; -.
DR   OrthoDB; 1107373at2; -.
DR   BioCyc; RSPH349102:G1G8M-2559-MON; -.
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_0000404702"
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;  34339 MW;  4847D452E39DFE0A CRC64;
     MSFRLQPPPP ARPNRCQLFG PGSRPALFEK MAASAADVVN LDLEDSVAPD DKAQARLNII
     EAINTLDWGK KYLSVRINGL DTPFWYRDVV DLLEQAGDRL DQIMIPKVGC AADVYAVDAL
     VTAIERAKGR TKPVSFEVII ESAAGIAHVE EIAAASPRLQ AMSLGAADFA ASMGMQTTGI
     GGTQENYYML HEGQKHWSDP WHWAQAAIVA ACRTHGILPV DGPFGDFSDD EGFRAQARRS
     ATLGMVGKWA IHPKQVALAN EVFTPSDKAV AEAREILAAM EAAKARGEGA TVYKGRLVDI
     ASIKQAEVIV RQAEMISA