MCLA_CHLAA
ID MCLA_CHLAA Reviewed; 348 AA.
AC A9WC35;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Malyl-CoA/beta-methylmalyl-CoA/citramalyl-CoA lyase;
DE EC=4.1.3.24;
DE EC=4.1.3.25;
DE AltName: Full=(3S)-3-carboxy-3-hydroxypropanoyl-CoA glyoxylate-lyase;
DE AltName: Full=(3S)-citramalyl-CoA pyruvate-lyase;
DE AltName: Full=(S)-citramalyl-CoA lyase;
DE AltName: Full=Erythro-beta-methylmalyl-CoA;
DE AltName: Full=L-malyl-CoA lyase;
GN Name=mclA; OrderedLocusNames=Caur_0174;
OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=324602;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
RX PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT "Complete genome sequence of the filamentous anoxygenic phototrophic
RT bacterium Chloroflexus aurantiacus.";
RL BMC Genomics 12:334-334(2011).
CC -!- FUNCTION: Involved in the 3-hydroxypropionate cycle used for
CC autotrophic carbon dioxide fixation, and in the glyoxylate assimilation
CC cycle used to regenerate acetyl-CoA and produce pyruvate as universal
CC precursor for biosynthesis. As a part of the 3-hydroxypropionate cycle,
CC it catalyzes the cleavage of (S)-malyl-CoA to yield acetyl-CoA and
CC glyoxylate. As part of the glyoxylate assimilation cycle, it catalyzes
CC the condensation of glyoxylate with propionyl-CoA to yield (2R,3S)-
CC beta-methylmalyl-CoA, and catalyzes the cleavage of (S)-citramalyl-CoA
CC to yield acetyl-CoA and pyruvate (By similarity). {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 -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-citramalyl-CoA = acetyl-CoA + pyruvate;
CC Xref=Rhea:RHEA:22612, ChEBI:CHEBI:15361, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:58668; EC=4.1.3.25;
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; CP000909; ABY33428.1; -; Genomic_DNA.
DR RefSeq; WP_012256084.1; NC_010175.1.
DR RefSeq; YP_001633817.1; NC_010175.1.
DR AlphaFoldDB; A9WC35; -.
DR SMR; A9WC35; -.
DR STRING; 324602.Caur_0174; -.
DR DNASU; 5824877; -.
DR EnsemblBacteria; ABY33428; ABY33428; Caur_0174.
DR KEGG; cau:Caur_0174; -.
DR PATRIC; fig|324602.8.peg.201; -.
DR eggNOG; COG2301; Bacteria.
DR HOGENOM; CLU_044864_0_1_0; -.
DR InParanoid; A9WC35; -.
DR OMA; AWLFCPA; -.
DR BioCyc; MetaCyc:MON-13604; -.
DR Proteomes; UP000002008; Chromosome.
DR GO; GO:0047777; F:(S)-citramalyl-CoA lyase activity; ISS:UniProtKB.
DR GO; GO:0043959; F:L-erythro-3-methylmalyl-CoA lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0050083; F:malyl-CoA lyase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
DR GO; GO:0043427; P:carbon fixation by 3-hydroxypropionate cycle; ISS:UniProtKB.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IBA:GO_Central.
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 Carbon dioxide fixation; Lyase; Magnesium; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..348
FT /note="Malyl-CoA/beta-methylmalyl-CoA/citramalyl-CoA lyase"
FT /id="PRO_0000429765"
FT BINDING 32..33
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 183..184
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 348 AA; 38367 MW; 3DE4A44F7D40151C CRC64;
MRKLAHNFYK PLAIGAPEPI RELPVRPERV VHFFPPHVEK IRARIPEVAK QVDVLCGNLE
DAIPMDAKEA ARNGFIEVVK ATDFGDTALW VRVNALNSPW VLDDIAEIVA AVGNKLDVIM
IPKVEGPWDI HFVDQYLALL EARHQIKKPI LIHALLETAQ GMVNLEEIAG ASPRMHGFSL
GPADLAASRG MKTTRVGGGH PFYGVLADPQ EGQAERPFYQ QDLWHYTIAR MVDVAVAHGL
RAFYGPFGDI KDEAACEAQF RNAFLLGCTG AWSLAPNQIP IAKRVFSPDV NEVLFAKRIL
EAMPDGSGVA MIDGKMQDDA TWKQAKVIVD LARMIAKKDP DLAQAYGL
