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Database: UniProt
Entry: A0A1J4V9R8_9BACT
LinkDB: A0A1J4V9R8_9BACT
Original site: A0A1J4V9R8_9BACT 
ID   A0A1J4V9R8_9BACT        Unreviewed;       522 AA.
AC   A0A1J4V9R8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE            EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN   ORFNames=AUJ70_02160 {ECO:0000313|EMBL:OIO33900.1};
OS   Candidatus Omnitrophica bacterium CG1_02_40_15.
OC   Bacteria; Candidatus Omnitrophota.
OX   NCBI_TaxID=1805284 {ECO:0000313|EMBL:OIO33900.1, ECO:0000313|Proteomes:UP000183570};
RN   [1] {ECO:0000313|EMBL:OIO33900.1, ECO:0000313|Proteomes:UP000183570}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG1_02_40_15 {ECO:0000313|EMBL:OIO33900.1};
RX   PubMed=27112493;
RA   Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA   Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT   "Genomic resolution of a cold subsurface aquifer community provides
RT   metabolic insights for novel microbes adapted to high CO concentrations.";
RL   Environ. Microbiol. 0:0-0(2016).
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}.
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:OIO33900.1}.
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DR   EMBL; MNVP01000041; OIO33900.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J4V9R8; -.
DR   STRING; 1805284.AUJ70_02160; -.
DR   UniPathway; UPA00047; UER00066.
DR   Proteomes; UP000183570; Unassembled WGS sequence.
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   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT   DOMAIN          4..270
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   522 AA;  57899 MW;  86D24AC46B67C574 CRC64;
     MRDIKIYDTT LRDGSQGEGI SFSVMDKVKI AKKLDKFGVH YIEGGWPGSN PKDMEFFKQA
     RKIKFKNSKL VAFGSTRRPK INPSDDENLK AIVKSGARLA AVFGKTWDMH VTDILKVSLQ
     ENLRMIKDTV EFLKSKNIYV FYDAEHFFDG YTRNKNYALE TLHSAISAGC DVVVLCDTNG
     GMLTHELGTI VRAISSECHA VTLGIHAHND GGLAVANTLA AVEAGASVAQ GTINGYGERC
     GNGDLCGIIP NLQLKMGYKC CSESKLKKLT EVSKYISEIS NMRPQDNQPF VGRSAFAHKG
     GVHINAVMKN SASYEHVMPE KVGNHRRILI SELSGKTSII LKAKEMELDL TKDDPKTKRI
     LRLIQSMENQ GYYFEAADGS FELLMKKVLK KYKPCFTLEG FKVSIEKRED DILISEAIIK
     LNVNKKEEHT AAIGDGPVNA LDNALRKALA KFYPTLSKMH LSDFKVRVLD EKAGTAAKVR
     VIIQSEDENS SWGTVGVSEN IIEASWQALV DSVEYKLLKD KA
//
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