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Database: UniProt
Entry: L8LS11_9CHRO
LinkDB: L8LS11_9CHRO
Original site: L8LS11_9CHRO 
ID   L8LS11_9CHRO            Unreviewed;       536 AA.
AC   L8LS11;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE            EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN   ORFNames=GLO73106DRAFT_00027440 {ECO:0000313|EMBL:ELR98905.1};
OS   Gloeocapsa sp. PCC 73106.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Chroococcaceae; Gloeocapsa.
OX   NCBI_TaxID=102232 {ECO:0000313|EMBL:ELR98905.1, ECO:0000313|Proteomes:UP000011180};
RN   [1] {ECO:0000313|EMBL:ELR98905.1, ECO:0000313|Proteomes:UP000011180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 73106 {ECO:0000313|EMBL:ELR98905.1,
RC   ECO:0000313|Proteomes:UP000011180};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA   Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA   Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA   Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT   genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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:ELR98905.1}.
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DR   EMBL; ALVY01000164; ELR98905.1; -; Genomic_DNA.
DR   RefSeq; WP_006528267.1; NZ_ALVY01000164.1.
DR   AlphaFoldDB; L8LS11; -.
DR   STRING; 102232.GLO73106DRAFT_00027440; -.
DR   PATRIC; fig|102232.3.peg.1292; -.
DR   eggNOG; COG0119; Bacteria.
DR   OrthoDB; 9804858at2; -.
DR   UniPathway; UPA00047; UER00066.
DR   Proteomes; UP000011180; 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:ARBA00022605};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011180};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT   DOMAIN          7..269
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   536 AA;  59194 MW;  7FC463B14C81A3A2 CRC64;
     MYQSNQIWLY DTTLRDGAQR EGISLSLEDK LKIVHKLDDM GIPFIEGGWP GANPKDVQFF
     WKLQEEPLKQ AQIVAFCSTR RPHKAVETDP MIESILDAGT TWVTIFGKSW ALQVTEGLNT
     TLEENLAMIG DTISYLRSQH KRVIYDAEHW FDGYKHNRDY ALLTLKTALD AGAEWLVFCD
     TNGGTLPHEI SEIVREIEPQ LQGNLGIHTH NDSGTAVANA LEAVRAGTRM VQGTFNGYGE
     RCGNANLCTV IPNLQLKMGY SCISPDKLVK LTETSRLISE IVNLAPDDHA PFVGRSAFAH
     KGGIHVSAVE RNPLTYEHIE PETIGNNRRI VISEQSGLSN VIAKARNFGI ELKKDDAASR
     QILERLKNLE NQGYQFEAAE ASFELLIRQS LGKRTEMFQL QGFQVHCDIF PGGENAANNA
     LATIKVAVNG KNLLEVAEGN GPVSALDQAL RKALVKFYPE IASFHLTDYK VRILDGDKGT
     AAKTRVLVES SNGEERWTTI GVSANILDAS YLAVVEGIEY GLLLASSITK PEKIAS
//
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