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
//