ID CCL_CHLAA Reviewed; 317 AA.
AC A9WGE2;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=(R)-citramalyl-CoA lyase;
DE EC=4.1.3.46;
GN Name=ccl; OrderedLocusNames=Caur_2265;
OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC Bacteria; Chloroflexota; 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).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, INDUCTION, COFACTOR, AND SUBUNIT.
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).
CC -!- FUNCTION: Involved in the glyoxylate assimilation cycle used to
CC regenerate acetyl-CoA and produce pyruvate as universal precursor for
CC biosynthesis. Catalyzes the cleavage of (R)-citramalyl-CoA to yield
CC acetyl-CoA and pyruvate. {ECO:0000269|PubMed:17259315}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-citramalyl-CoA = acetyl-CoA + pyruvate;
CC Xref=Rhea:RHEA:38275, ChEBI:CHEBI:15361, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:75637; EC=4.1.3.46;
CC Evidence={ECO:0000269|PubMed:17259315};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17259315};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:17259315};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:17259315};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17259315};
CC Note=Divalent cations such as manganese, cobalt, nickel and magnesium.
CC {ECO:0000269|PubMed:17259315};
CC -!- ACTIVITY REGULATION: Activated by dithioerythritol (DTE) (in vitro).
CC {ECO:0000269|PubMed:17259315}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=280 nm {ECO:0000269|PubMed:17259315};
CC Kinetic parameters:
CC KM=70 uM for (R)-citramalyl-CoA {ECO:0000269|PubMed:17259315};
CC Note=kcat is 1.7 sec(-1) for lyase activity with (R)-citramalyl-CoA
CC as substrate.;
CC pH dependence:
CC Optimum pH is 7 (at 55 degrees Celsius).
CC {ECO:0000269|PubMed:17259315};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:17259315};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17259315}.
CC -!- INDUCTION: Under autotrophic growth conditions.
CC {ECO:0000269|PubMed:17259315}.
CC -!- SIMILARITY: Belongs to the HMG-CoA lyase family. {ECO:0000305}.
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DR EMBL; CP000909; ABY35474.1; -; Genomic_DNA.
DR RefSeq; WP_012258128.1; NC_010175.1.
DR RefSeq; YP_001635863.1; NC_010175.1.
DR AlphaFoldDB; A9WGE2; -.
DR SMR; A9WGE2; -.
DR STRING; 324602.Caur_2265; -.
DR EnsemblBacteria; ABY35474; ABY35474; Caur_2265.
DR KEGG; cau:Caur_2265; -.
DR PATRIC; fig|324602.8.peg.2566; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022138_3_2_0; -.
DR InParanoid; A9WGE2; -.
DR Proteomes; UP000002008; Chromosome.
DR GO; GO:0044101; F:(3R)-citramalyl-CoA lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0004419; F:hydroxymethylglutaryl-CoA lyase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016833; F:oxo-acid-lyase activity; IDA:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0043427; P:carbon fixation by 3-hydroxypropionate cycle; IDA:UniProtKB.
DR GO; GO:0009436; P:glyoxylate catabolic process; IDA:UniProtKB.
DR GO; GO:0046951; P:ketone body biosynthetic process; IBA:GO_Central.
DR GO; GO:0006552; P:leucine catabolic process; IBA:GO_Central.
DR CDD; cd07938; DRE_TIM_HMGL; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR043594; HMGL.
DR InterPro; IPR000891; PYR_CT.
DR PANTHER; PTHR42738; HYDROXYMETHYLGLUTARYL-COA LYASE; 1.
DR PANTHER; PTHR42738:SF7; HYDROXYMETHYLGLUTARYL-COA LYASE; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding; Pyruvate; Reference proteome; Transferase.
FT CHAIN 1..317
FT /note="(R)-citramalyl-CoA lyase"
FT /id="PRO_0000429587"
FT DOMAIN 4..281
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT ACT_SITE 247
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 13
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
SQ SEQUENCE 317 AA; 33648 MW; 2007AEBBAB93829B CRC64;
MEAVTIVDVA PRDGLQNEPD VLEPATRVEL IERLLAAGVP RIEIGSFVNP RQVPQMAGID
QIARMLIERG HNLAARTTND LFRFTALVPN QRGYELAAAA GLRHVRLVLA ASDGLNRANF
KRTTAESLIE FSRFALNIRR DGLTFGVAIG AAFGCPFDGY VSPERVRAIA EHAVDIGAGE
IILADTTGMA VPTQVAALCR TILDRIPDVT VTLHLHNTRN TGYANAFAAW QVGIRSFDAA
LGGIGGCPFA PRAVGNIASE DLVHLFNGLG VPTGIDLSAL IAASDWLSAT LGRPLPALVG
KAGPVYPQVV SMAPYLS
//
