ID A0A0Q1AHG4_9EURY Unreviewed; 502 AA.
AC A0A0Q1AHG4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Putative (R)-citramalate synthase CimA {ECO:0000256|HAMAP-Rule:MF_01028};
DE EC=2.3.3.21 {ECO:0000256|HAMAP-Rule:MF_01028};
GN Name=cimA {ECO:0000256|HAMAP-Rule:MF_01028};
GN ORFNames=APR55_06765 {ECO:0000313|EMBL:KQC03732.1};
OS Methanolinea sp. SDB.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanolinea.
OX NCBI_TaxID=1735327 {ECO:0000313|EMBL:KQC03732.1, ECO:0000313|Proteomes:UP000050878};
RN [1] {ECO:0000313|EMBL:KQC03732.1, ECO:0000313|Proteomes:UP000050878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDB {ECO:0000313|EMBL:KQC03732.1};
RA Wawrik B., Marks C.R., Davidova I.A., Mcinerney M.J., Pruitt S., Duncan K.,
RA Suflita J.M., Callaghan A.V.;
RT "Metagenomic Analysis of a Methanogenic Paraffin-Utilizing Consortium.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the condensation of pyruvate and acetyl-coenzyme A
CC to form (R)-citramalate. {ECO:0000256|HAMAP-Rule:MF_01028}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + H2O + pyruvate = (3R)-citramalate + CoA + H(+);
CC Xref=Rhea:RHEA:19045, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30934, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288; EC=2.3.3.21; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01028};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC oxobutanoate from pyruvate: step 1/3. {ECO:0000256|HAMAP-
CC Rule:MF_01028}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01028}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|ARBA:ARBA00006154, ECO:0000256|HAMAP-
CC Rule:MF_01028, ECO:0000256|RuleBase:RU003523}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQC03732.1}.
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DR EMBL; LKUF01000462; KQC03732.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q1AHG4; -.
DR UniPathway; UPA00047; UER00066.
DR Proteomes; UP000050878; Unassembled WGS sequence.
DR GO; GO:0043714; F:(R)-citramalate synthase activity; IEA:InterPro.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro.
DR CDD; cd07940; DRE_TIM_IPMS; 1.
DR Gene3D; 1.10.238.260; -; 1.
DR Gene3D; 3.30.160.270; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_01028; CimA; 1.
DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR024890; Citramalate_synthase_CimA.
DR InterPro; IPR011830; LEU1_arch.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR000891; PYR_CT.
DR NCBIfam; TIGR02090; LEU1_arch; 1.
DR PANTHER; PTHR42880:SF2; (R)-CITRAMALATE SYNTHASE CIMA; 1.
DR PANTHER; PTHR42880; HOMOCITRATE SYNTHASE; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF08502; LeuA_dimer; 1.
DR SMART; SM00917; LeuA_dimer; 1.
DR SUPFAM; SSF110921; 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01028};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|HAMAP-Rule:MF_01028};
KW Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624, ECO:0000256|HAMAP-
KW Rule:MF_01028};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01028}.
FT DOMAIN 8..256
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 502 AA; 54405 MW; 03BB00303725317C CRC64;
MVLFTEKIRF FDTTLRDGEQ TPGVSLKPTD KLEIATRLAE IGVDVIEVGS AAASEGERQA
IRIISDAGLS AEICTYVRAM KGDIDYAADF GADSVHLVVP VSDLHIEKKM RKTRADICTM
AFSAVEYAKE RGLIVELSGE DASRADTGFL YDVYAGGLEV GADRLCFCDT VGLLTPERVA
EIIPPLCIAP LSIHCHDDLG FSLANTMAAL RAGATCAHAT VNGLGERAGN TPFEELVMSL
EVLYGYKTGI RKEQIYQLSS VVSRLTDIPL PTNKAIVGEM AFTHESGIHA HGVLREPSTY
EPVKPETIGR RRRILLGKHS GKAAVEAALN EMNYYPDETQ LQEILKRIKD LGDRGMRITD
ADMMAVTEAV MAIECRPVLK MRQFTVVSGS NVIPTASVTL LVRDEEITGA ATGTGPVDAA
MEALRRSVAA VADIRLEEYH VDAIHGGTDA LVDVTVRLSK DGKIITSRGA RTDIIMASVE
AVIAGMNRLL REEDENRSKN PD
//
