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Entry: A0A0F5YK77_9CYAN
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ID   A0A0F5YK77_9CYAN        Unreviewed;       540 AA.
AC   A0A0F5YK77;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE            EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN   ORFNames=WN50_04155 {ECO:0000313|EMBL:KKD39329.1};
OS   Limnoraphis robusta CS-951.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Sirenicapillariaceae; Limnoraphis.
OX   NCBI_TaxID=1637645 {ECO:0000313|EMBL:KKD39329.1, ECO:0000313|Proteomes:UP000033607};
RN   [1] {ECO:0000313|EMBL:KKD39329.1, ECO:0000313|Proteomes:UP000033607}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CS-951 {ECO:0000313|EMBL:KKD39329.1,
RC   ECO:0000313|Proteomes:UP000033607};
RA   Willis A., Parks M., Burford M.A.;
RT   "Draft genome assembly of filamentous brackish cyanobacterium Limnoraphis
RT   robusta strain CS-951.";
RL   Submitted (JUN-2015) 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}.
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:KKD39329.1}.
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DR   EMBL; LATL02000181; KKD39329.1; -; Genomic_DNA.
DR   RefSeq; WP_046277237.1; NZ_LATL02000181.1.
DR   AlphaFoldDB; A0A0F5YK77; -.
DR   PATRIC; fig|1637645.4.peg.3626; -.
DR   OrthoDB; 9804858at2; -.
DR   UniPathway; UPA00047; UER00066.
DR   Proteomes; UP000033607; 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   Reference proteome {ECO:0000313|Proteomes:UP000033607};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT   DOMAIN          6..275
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   540 AA;  59514 MW;  1EDACC5FBB0D185B CRC64;
     MTHPTCWIYD TTLRDGAQRE GISLSIEDKL RIAHRLDALG IPFIEGGWPG ANPKDVQFFW
     RLQEEPLTQA EVVAFCSTRR PGTTAATEPA FKPILSARTR WVTIFGKSWD LQVTEGLKTS
     LEENLAMIGD SIEFLIAQGR RMIYDAEHWF DGYKQNPDYA LKTLEAAARA GAEWLVLCDT
     NGGTLPHEVS EITRQVVEAV ASWNLDPIPQ IGIHTHNDSG TAVANALAAV RSGARMVQGT
     INGYGERCGN ANLCTVIPNL QLKLGYSCIG EDKIIKLTET SRLVSELVNL APDEHAPFVG
     LSAFAHKGGI HVSAVQRNPL TYEHIEPETV GNKRRIVISE QSGLSNVLIK AQSFGIELDR
     DHPTCRQILQ RLKELEHQGY QFEAAEASFE LLMREALLTR QSLFEIKGFQ VHCDKRTSDM
     SNSLATVKVT VNGEEILASA EGNGPVSALD SALRKALLSF YPAIAQFQLT DYKVRILDGR
     EGTSAKTRVL IESSNGQKRW TTVGVSTNIL DASYQAVVEG LEYGLLLTQT QQNPVSLKLS
//
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