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Database: UniProt
Entry: B0K7V2_THEP3
LinkDB: B0K7V2_THEP3
Original site: B0K7V2_THEP3 
ID   B0K7V2_THEP3            Unreviewed;       520 AA.
AC   B0K7V2;
DT   18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT   18-MAR-2008, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE            EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN   OrderedLocusNames=Teth39_0689 {ECO:0000313|EMBL:ABY94351.1};
OS   Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium
OS   thermohydrosulfuricum).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=340099 {ECO:0000313|EMBL:ABY94351.1, ECO:0000313|Proteomes:UP000002156};
RN   [1] {ECO:0000313|Proteomes:UP000002156}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33223 / DSM 2355 / 39E
RC   {ECO:0000313|Proteomes:UP000002156};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z., Zhou J.,
RA   Richardson P.;
RT   "Complete sequence of Thermoanaerobacter pseudethanolicus 39E.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00034270};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC       oxobutanoate from pyruvate: step 1/3. {ECO:0000256|ARBA:ARBA00004743}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. {ECO:0000256|ARBA:ARBA00006154, ECO:0000256|RuleBase:RU003523}.
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DR   EMBL; CP000924; ABY94351.1; -; Genomic_DNA.
DR   RefSeq; WP_012269134.1; NC_010321.1.
DR   AlphaFoldDB; B0K7V2; -.
DR   STRING; 340099.Teth39_0689; -.
DR   KEGG; tpd:Teth39_0689; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_022158_7_0_9; -.
DR   OMA; KSWDFHV; -.
DR   UniPathway; UPA00047; UER00066.
DR   Proteomes; UP000002156; Chromosome.
DR   GO; GO:0043714; F:(R)-citramalate synthase activity; IEA:RHEA.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:InterPro.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro.
DR   CDD; cd07941; DRE_TIM_LeuA3; 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   InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005675; Citramal_synthase.
DR   InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR   InterPro; IPR000891; PYR_CT.
DR   NCBIfam; TIGR00977; citramal_synth; 1.
DR   PANTHER; PTHR43538:SF1; (R)-CITRAMALATE SYNTHASE; 1.
DR   PANTHER; PTHR43538; ALPHA-IPM SYNTHASE/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   Acyltransferase {ECO:0000313|EMBL:ABY94351.1};
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624};
KW   Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002156};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT   DOMAIN          4..269
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   520 AA;  57675 MW;  BD5517AA27AF725C CRC64;
     MRNIRIYDTT LRDGVQGQGI SFTVEDKLKI VKVLDEFGVA YIEAGNPGSN PKDIEFFERV
     KSIKLKNAKL IAFGSTRRAN TTTKEDANVI SLLNADTEVV TIFGKSWDFQ VTEILKTTLE
     ENLKMIYDTV KFFKDKGKSV IFDAEHFFDG YKQNPEYALK TLEVALEAGV DSVCLCDTKG
     GAFPMEVYDI TKTVVDKFNT EVGIHCHNDN GMAVADSIMA VQAGAIQLQG TINGYGERCG
     NANLCTLIPN LQLLMGYKCV PDENLKQLTH LARFVSEIAN VTYDERAPYV GKNAFSHKAG
     MHADAVNKNT YSYELIDPSL VGNSRTFLIS EVAGRGTVLN AINEIDPTIT KDSPETKLIL
     DKLKEMEYLG YQYENAGGSL ELLIRKVLGK YKPAFNLKEF KVIVNEPSVN SVNSSALIKV
     EVDSIEEIAA AEGDGPVHAL DNAVRRVLER FYPQIKEMRL TDYKVRVLDS NSATAAKVRV
     IIESTDGKDS WSTIGVSTDI IEASWRALVD SIEYKLNKES
//
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