MCLA_CHLAU
ID MCLA_CHLAU Reviewed; 348 AA.
AC S5N020;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 03-AUG-2022, entry version 33.
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=mcl;
OS Chloroflexus aurantiacus.
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=1108;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=DSM 636 / OK-70-fl;
RX PubMed=12374834; DOI=10.1128/jb.184.21.5999-6006.2002;
RA Herter S., Busch A., Fuchs G.;
RT "L-Malyl-coenzyme A lyase/beta-methylmalyl-coenzyme A lyase from
RT Chloroflexus aurantiacus, a bifunctional enzyme involved in autotrophic
RT CO(2) fixation.";
RL J. Bacteriol. 184:5999-6006(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A CITRAMALYL-COA LYASE, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=DSM 636 / OK-70-fl;
RX PubMed=19955419; DOI=10.1073/pnas.0908356106;
RA Zarzycki J., Brecht V., Muller M., Fuchs G.;
RT "Identifying the missing steps of the autotrophic 3-hydroxypropionate CO2
RT fixation cycle in Chloroflexus aurantiacus.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:21317-21322(2009).
RN [3]
RP FUNCTION.
RC STRAIN=DSM 636 / OK-70-fl;
RX PubMed=17259315; DOI=10.1128/jb.01620-06;
RA Friedmann S., Alber B.E., Fuchs G.;
RT "Properties of R-citramalyl-coenzyme A lyase and its role in the
RT autotrophic 3-hydroxypropionate cycle of Chloroflexus aurantiacus.";
RL J. Bacteriol. 189:2906-2914(2007).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS
RP ANS MAGNESIUM ION, FUNCTION, ACTIVITY REGULATION, COFACTOR, AND SUBUNIT.
RX PubMed=24206647; DOI=10.1186/1472-6807-13-28;
RA Zarzycki J., Kerfeld C.A.;
RT "The crystal structures of the tri-functional Chloroflexus aurantiacus and
RT bi-functional Rhodobacter sphaeroides malyl-CoA lyases and comparison with
RT CitE-like superfamily enzymes and malate synthases.";
RL BMC Struct. Biol. 13:28-28(2013).
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. {ECO:0000269|PubMed:12374834,
CC ECO:0000269|PubMed:17259315, ECO:0000269|PubMed:19955419,
CC ECO:0000269|PubMed:24206647}.
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:12374834};
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:12374834};
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 Evidence={ECO:0000269|PubMed:12374834};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:24206647};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:24206647};
CC Note=Divalent cations such as magnesium or manganese.
CC {ECO:0000269|PubMed:24206647};
CC -!- ACTIVITY REGULATION: Inhibited by oxalate.
CC {ECO:0000269|PubMed:12374834, ECO:0000269|PubMed:24206647}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 uM for (S)-malyl-CoA (for L-malyl-CoA lyase activity)
CC {ECO:0000269|PubMed:12374834, ECO:0000269|PubMed:19955419};
CC KM=89 uM for (2R,3S)-beta-methylmalyl-CoA (for beta-methylmalyl-CoA
CC lyase activity) {ECO:0000269|PubMed:12374834,
CC ECO:0000269|PubMed:19955419};
CC KM=360 uM for acetyl-CoA (for L-malyl-CoA lyase activity)
CC {ECO:0000269|PubMed:12374834, ECO:0000269|PubMed:19955419};
CC KM=1200 uM for propionyl-CoA (for beta-methylmalyl-CoA lyase
CC activity) {ECO:0000269|PubMed:12374834, ECO:0000269|PubMed:19955419};
CC KM=2000 uM for glyoxylate (for beta-methylmalyl-CoA and L-malyl-CoA
CC lyase activities) {ECO:0000269|PubMed:12374834,
CC ECO:0000269|PubMed:19955419};
CC pH dependence:
CC Optimum pH is 7.1. {ECO:0000269|PubMed:12374834,
CC ECO:0000269|PubMed:19955419};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.
CC {ECO:0000269|PubMed:12374834, ECO:0000269|PubMed:19955419};
CC -!- SUBUNIT: Homohexamer. Dimer of trimers. {ECO:0000269|PubMed:12374834,
CC ECO:0000269|PubMed:24206647}.
CC -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family. {ECO:0000305}.
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DR EMBL; KF240561; AGR55786.1; -; Genomic_DNA.
DR PDB; 4L7Z; X-ray; 2.50 A; A/B/C/D/E/F=1-348.
DR PDB; 4L80; X-ray; 2.01 A; A/B/C/D/E/F=1-348.
DR PDBsum; 4L7Z; -.
DR PDBsum; 4L80; -.
DR AlphaFoldDB; S5N020; -.
DR SMR; S5N020; -.
DR OMA; AWLFCPA; -.
DR BRENDA; 4.1.3.24; 1352.
DR BRENDA; 4.1.3.25; 1352.
DR GO; GO:0047777; F:(S)-citramalyl-CoA lyase activity; IDA:UniProtKB.
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 GO; GO:0043427; P:carbon fixation by 3-hydroxypropionate cycle; 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 3D-structure; Carbon dioxide fixation; Lyase; Magnesium; Manganese;
KW Metal-binding.
FT CHAIN 1..348
FT /note="Malyl-CoA/beta-methylmalyl-CoA/citramalyl-CoA lyase"
FT /id="PRO_0000429764"
FT BINDING 32..33
FT /ligand="substrate"
FT BINDING 40
FT /ligand="substrate"
FT BINDING 92
FT /ligand="substrate"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24206647,
FT ECO:0007744|PDB:4L80"
FT BINDING 183..184
FT /ligand="substrate"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24206647,
FT ECO:0007744|PDB:4L80"
FT BINDING 274
FT /ligand="substrate"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:4L80"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:4L80"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:4L80"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:4L80"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:4L80"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:4L80"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:4L80"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:4L7Z"
FT HELIX 101..112
FT /evidence="ECO:0007829|PDB:4L80"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:4L80"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:4L80"
FT HELIX 127..143
FT /evidence="ECO:0007829|PDB:4L80"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:4L80"
FT HELIX 159..163
FT /evidence="ECO:0007829|PDB:4L80"
FT HELIX 165..169
FT /evidence="ECO:0007829|PDB:4L80"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:4L80"
FT HELIX 182..189
FT /evidence="ECO:0007829|PDB:4L80"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:4L80"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:4L80"
FT HELIX 225..237
FT /evidence="ECO:0007829|PDB:4L80"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:4L80"
FT HELIX 253..266
FT /evidence="ECO:0007829|PDB:4L80"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:4L80"
FT HELIX 278..285
FT /evidence="ECO:0007829|PDB:4L80"
FT HELIX 290..302
FT /evidence="ECO:0007829|PDB:4L80"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:4L7Z"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:4L80"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:4L80"
FT HELIX 319..336
FT /evidence="ECO:0007829|PDB:4L80"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:4L80"
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
