ID A0A0K2LTK9_9NOST Unreviewed; 559 AA.
AC A0A0K2LTK9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN ORFNames=AA650_00275 {ECO:0000313|EMBL:ALB39097.1};
OS Anabaena sp. WA102.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX NCBI_TaxID=1647413 {ECO:0000313|EMBL:ALB39097.1, ECO:0000313|Proteomes:UP000056652};
RN [1] {ECO:0000313|EMBL:ALB39097.1, ECO:0000313|Proteomes:UP000056652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WA102 {ECO:0000313|EMBL:ALB39097.1,
RC ECO:0000313|Proteomes:UP000056652};
RA Brown N.M.;
RT "The finished genome of an anatoxin-a-producing Anabaena isolate reveals
RT extensive genome rearrangement.";
RL Submitted (MAY-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}.
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DR EMBL; CP011456; ALB39097.1; -; Genomic_DNA.
DR RefSeq; WP_053537505.1; NZ_CP011456.1.
DR AlphaFoldDB; A0A0K2LTK9; -.
DR STRING; 1647413.AA650_00275; -.
DR KEGG; awa:AA650_00275; -.
DR PATRIC; fig|1647413.5.peg.65; -.
DR OrthoDB; 570404at2; -.
DR UniPathway; UPA00047; UER00066.
DR Proteomes; UP000056652; Chromosome.
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; 2.
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; 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 9..296
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 559 AA; 61418 MW; BF461B99954FCFDD CRC64;
MTKTPSNQLW LYDTTLRDGT QREGLSVSIE DKLRIAHKLD ELGIPFIEGG WPGANPKDVQ
FFWQLRENPL KQAEVVPFCS TRRPHTKAGD EPMLQGILAA GTRWVTIFGK SWDLHVTTGL
KTSLEENLAM IGDTIEYLRS QGRRVIYDAE HWFDGYKQNP DYALQTLKAA VTAGAEWLVL
CDTNGGTLPH EVSQIVEDVV KGTGDWGLGT GNEEKTLTQS PITNHQLPLP KIGIHTHNDS
EMAVANALAA VMAGAKMVQG TINGYGERCG NANLCSVIPN LQLKLGYSCI GEHQLNQLTE
ASRFVSEVVN LAPDEHAPFV GLSAFAHKGG IHVSAVERNP LTYEHIQPEL VGNQRRIVIS
EQSGLSNVLA KAKTCGIELD KDHPQARQIL QRMKELESEG YQFEAAEASF ILLMYEALSC
RQQFFEVQGF QVHCDLVEVK ETTNSLATVK VAVNGKNILE AAEGNGPVAA LDAALRKALV
NFYPQIADFE LTDYKVRILN GNTGTSAKTR ALVESGNGQQ RWTTVGVSSN ILEASYQAVV
EGLEYGLLLH FQAEKTLKV
//
