ID   MCAL_RHOCB              Reviewed;         318 AA.
AC   D5AR83;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=L-malyl-CoA/beta-methylmalyl-CoA lyase {ECO:0000250|UniProtKB:B6E2X2};
DE            EC=4.1.3.24 {ECO:0000250|UniProtKB:B6E2X2};
DE   AltName: Full=(3S)-malyl-CoA/beta-methylmalyl-CoA lyase {ECO:0000250|UniProtKB:Q3J5L6};
GN   Name=mcl1 {ECO:0000250|UniProtKB:Q3J5L6}; OrderedLocusNames=RCAP_rcc03164;
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272942;
RN   [1] {ECO:0000312|EMBL:ADE86888.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=20418398; DOI=10.1128/jb.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT   Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(2010).
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.
CC       {ECO:0000250|UniProtKB:B6E2X2}.
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         Evidence={ECO:0000250|UniProtKB:B6E2X2};
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         Evidence={ECO:0000250|UniProtKB:B6E2X2};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:B6E2X2};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:B6E2X2};
CC       Note=Divalent cations such as magnesium or manganese.
CC       {ECO:0000250|UniProtKB:B6E2X2};
CC   -!- SUBUNIT: Homohexamer. Dimer of trimers. {ECO:0000250|UniProtKB:B6E2X2}.
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family. {ECO:0000305}.
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DR   EMBL; CP001312; ADE86888.1; -; Genomic_DNA.
DR   RefSeq; WP_013068861.1; NC_014034.1.
DR   AlphaFoldDB; D5AR83; -.
DR   SMR; D5AR83; -.
DR   STRING; 272942.RCAP_rcc03164; -.
DR   EnsemblBacteria; ADE86888; ADE86888; RCAP_rcc03164.
DR   GeneID; 31491951; -.
DR   KEGG; rcp:RCAP_rcc03164; -.
DR   eggNOG; COG2301; Bacteria.
DR   HOGENOM; CLU_044864_0_1_5; -.
DR   OMA; WDIHYLD; -.
DR   OrthoDB; 1107373at2; -.
DR   Proteomes; UP000002361; Chromosome.
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; Reference proteome.
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_0000404700"
FT   BINDING         19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3J5L6"
FT   BINDING         24
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3J5L6"
FT   BINDING         30
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3J5L6"
FT   BINDING         76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3J5L6"
FT   BINDING         141
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q3J5L6"
FT   BINDING         167..168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3J5L6"
FT   BINDING         168
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q3J5L6"
FT   BINDING         251..252
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3J5L6"
SQ   SEQUENCE   318 AA;  34248 MW;  521EE8E036162994 CRC64;
     MSFRTQPPAP ARLNRCQLFG PGSRPAIFEK MAQSAADVIN LDLEDSVAPD DKPQARRNII
     EASHNIDWGN KYLSVRINGL DTPFWYRDVV ELLEDGSERI DQIMIPKVGC AADVYAVDAL
     VTAIEAAKGR KKRISLEVII ESAAGIAHVE EIAAASPRLQ AMSLGAADFA ASMGMATTGI
     GGTQENYYML HAGVKHWSDP WHWAQAAIVA ACRTHGILPV DGPFGDFSDD EGFRAQALRS
     ATLGMVGKWA IHPKQVALAN EVFTPSDAAV AEAREILAAM EKAKAEGAGA TVYKGRLVDI
     ASIRQAEVIV RQAEMAKV