MCAL_RHOCA
ID MCAL_RHOCA Reviewed; 318 AA.
AC B6E2X2;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=L-malyl-CoA/beta-methylmalyl-CoA lyase {ECO:0000312|EMBL:ACI22682.1};
DE EC=4.1.3.24 {ECO:0000269|PubMed:15687206};
DE AltName: Full=(3S)-malyl-CoA/beta-methylmalyl-CoA lyase {ECO:0000250|UniProtKB:Q3J5L6};
GN Name=mcl1 {ECO:0000250|UniProtKB:Q3J5L6};
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1] {ECO:0000312|EMBL:ACI22682.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33303 / B10 {ECO:0000312|EMBL:ACI22682.1};
RA Alber B.E., Meister M., Fuchs G.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-8, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 33303 / B10 {ECO:0000269|PubMed:15687206};
RX PubMed=15687206; DOI=10.1128/jb.187.4.1415-1425.2005;
RA Meister M., Saum S., Alber B.E., Fuchs G.;
RT "L-malyl-coenzyme A/beta-methylmalyl-coenzyme A lyase is involved in
RT acetate assimilation of the isocitrate lyase-negative bacterium Rhodobacter
RT capsulatus.";
RL J. Bacteriol. 187:1415-1425(2005).
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 beta-methylmalyl-CoA.
CC {ECO:0000269|PubMed:15687206}.
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:0000269|PubMed:15687206};
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:0000269|PubMed:15687206};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15687206};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:15687206};
CC Note=Divalent cations such as magnesium or manganese.
CC {ECO:0000269|PubMed:15687206};
CC -!- ACTIVITY REGULATION: In vitro inhibited by EDTA.
CC {ECO:0000269|PubMed:15687206}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15 uM for L-malyl-CoA {ECO:0000269|PubMed:15687206};
CC KM=21 uM for beta-methylmalyl-CoA {ECO:0000269|PubMed:15687206};
CC KM=0.14 mM for acetyl-CoA {ECO:0000269|PubMed:15687206};
CC KM=1.2 mM for glyoxylate {ECO:0000269|PubMed:15687206};
CC -!- SUBUNIT: Homohexamer. Dimer of trimers. {ECO:0000269|PubMed:15687206}.
CC -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family. {ECO:0000305}.
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DR EMBL; FJ200073; ACI22682.1; -; Genomic_DNA.
DR RefSeq; WP_013068861.1; NZ_VIBE01000005.1.
DR AlphaFoldDB; B6E2X2; -.
DR SMR; B6E2X2; -.
DR GeneID; 31491951; -.
DR BioCyc; MetaCyc:MON-13588; -.
DR GO; GO:0043959; F:L-erythro-3-methylmalyl-CoA lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0050083; F:malyl-CoA lyase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IDA: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 1: Evidence at protein level;
KW Direct protein sequencing; Lyase; Magnesium; Manganese; Metal-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15687206"
FT CHAIN 2..318
FT /note="L-malyl-CoA/beta-methylmalyl-CoA lyase"
FT /id="PRO_0000404699"
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
