ID R4M3C0_MYCTX Unreviewed; 486 AA.
AC R4M3C0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN ORFNames=I917_26010 {ECO:0000313|EMBL:AGL25250.1};
OS Mycobacterium tuberculosis str. Haarlem/NITR202.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=1304279 {ECO:0000313|EMBL:AGL25250.1, ECO:0000313|Proteomes:UP000013563};
RN [1] {ECO:0000313|EMBL:AGL25250.1, ECO:0000313|Proteomes:UP000013563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Haarlem/NITR202 {ECO:0000313|EMBL:AGL25250.1,
RC ECO:0000313|Proteomes:UP000013563};
RX PubMed=23788533;
RA Narayanan S., Deshpande U.;
RT "Whole-Genome Sequences of Four Clinical Isolates of Mycobacterium
RT tuberculosis from Tamil Nadu, South India.";
RL Genome Announc. 1:e00186-13(2013).
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004689}.
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DR EMBL; CP004886; AGL25250.1; -; Genomic_DNA.
DR KEGG; mtuh:I917_26010; -.
DR PATRIC; fig|1304279.3.peg.5300; -.
DR HOGENOM; CLU_004588_3_2_11; -.
DR BioCyc; MTUB1304279:G13AB-3521-MONOMER; -.
DR Proteomes; UP000013563; Chromosome.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd07942; DRE_TIM_LeuA; 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; IPR013785; Aldolase_TIM.
DR InterPro; IPR005668; IPM_Synthase.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR039371; LeuA_N_DRE-TIM.
DR InterPro; IPR000891; PYR_CT.
DR NCBIfam; TIGR00970; leuA_yeast; 1.
DR PANTHER; PTHR46911; -; 1.
DR PANTHER; PTHR46911:SF1; 2-ISOPROPYLMALATE SYNTHASE; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF08502; LeuA_dimer; 1.
DR SUPFAM; SSF110921; 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:AGL25250.1};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AGL25250.1}.
FT DOMAIN 1..257
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 486 AA; 53661 MW; F4F273430DD608F5 CRC64;
MSPARKRRMF DLLVRMGYKE IEVGFPSASQ TDFDFVREII EQGAIPDDVT IQVLTQCRPE
LIERTFQACS GAPRAIVHFY NSTSILQRRV VFRANRAEVQ AIATDGARKC VEQAAKYPGT
QWRFEYSPES YTGTELEYAK QVCDAVGEVI APXPERPIIF XLPATVEMTT PNVYADSIEW
MSRNLANRES VILSLHPHNX RGTAVAAAEL GFAAGADRIE GCLFGNGERT GNVCLVTLGL
NLFSRGVDPQ IDFSNIDEIR RTVEYCNQLP VHERHPYGGD LVYTAFSGSH QDAINKGLDA
MKLDADAADC DVDDMLWQVP YLPIDPRDVG RTYEAVIRVN SQSGKGGVAY IMKTDHGLSL
PRRLQIEFSQ VIQKIAEGTA GEGGEVSPKE MWDAFAEEYL APVRPLERIR QHVDAADDDG
GTTSITATVK INGVETEISG SGNGPLAAFV HALADVGFDG GRAGLXRARD ERRRRRSGRR
VXWXPP
//
