ID A0A0G0JKS2_9BACT Unreviewed; 475 AA.
AC A0A0G0JKS2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00018198};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN ORFNames=US54_C0036G0008 {ECO:0000313|EMBL:KKQ37344.1};
OS Candidatus Roizmanbacteria bacterium GW2011_GWA2_37_7.
OC Bacteria; Candidatus Roizmanbacteria.
OX NCBI_TaxID=1618481 {ECO:0000313|EMBL:KKQ37344.1, ECO:0000313|Proteomes:UP000034471};
RN [1] {ECO:0000313|EMBL:KKQ37344.1, ECO:0000313|Proteomes:UP000034471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004689}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 1 subfamily. {ECO:0000256|ARBA:ARBA00009396}.
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:KKQ37344.1}.
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DR EMBL; LBTJ01000036; KKQ37344.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0JKS2; -.
DR STRING; 1618481.US54_C0036G0008; -.
DR PATRIC; fig|1618481.3.peg.718; -.
DR Proteomes; UP000034471; Unassembled WGS sequence.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:InterPro.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd07940; DRE_TIM_IPMS; 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; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR000891; PYR_CT.
DR PANTHER; PTHR10277:SF9; 2-ISOPROPYLMALATE SYNTHASE 1, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR10277; HOMOCITRATE SYNTHASE-RELATED; 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 Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 17..277
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 475 AA; 52413 MW; B7E5EE235918634C CRC64;
MSSQDVLRFL LHNMQKVQIF DTTLRDGEQV PGCQLNTVEK IEIAKALESL GVDIIEAGFP
ISSPCDFQSV IEISKVVKKP VICALTRAVK GDIDAAVASL QFAKKKRIHT GIGASDIHIK
YKFKSTRKDI LQRGIEAVKY AKKFVEDIEF YAEDAGRADL EFLSQMIEAV INAGATVVNI
PDTTGYNLPH VYGAKIKYLK EHVSNIHKAI ISVHCHNDLG LATANAMAGI ENGARQVEAT
VNGIGERAGN TSLEEVVMIM RTHKLAYDTH INTKKIYPTS RLVSKLMNMP VQPNKAIVGK
NAFAHSSGIH QDGILKQREN YEIIDPYEKF LELADSKKHI NDEDLHMLMG KTLIVQKKLQ
IELIEVVCGF PLKPMATVKM RIDGVEHKAV ANGNGPVDAS YKAVNQVITQ AGILKTLPIL
QEFLIQALTK GSDDVSKVNV QLEYKDTIYY GFGSDTDIVV ASVWAYVDGI NKIIS
//
