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Database: UniProt
Entry: M3GDB3_LEPBO
LinkDB: M3GDB3_LEPBO
Original site: M3GDB3_LEPBO 
ID   M3GDB3_LEPBO            Unreviewed;       110 AA.
AC   M3GDB3;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE            EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN   ORFNames=LEP1GSC123_3192 {ECO:0000313|EMBL:EMF98921.1};
OS   Leptospira borgpetersenii str. 200701203.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1193007 {ECO:0000313|EMBL:EMF98921.1, ECO:0000313|Proteomes:UP000011783};
RN   [1] {ECO:0000313|EMBL:EMF98921.1, ECO:0000313|Proteomes:UP000011783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=200701203 {ECO:0000313|EMBL:EMF98921.1,
RC   ECO:0000313|Proteomes:UP000011783};
RA   Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA   Sanka R., DePew J., Purushe J., Picardeau M., Werts C., Goarant C.,
RA   Vinetz J.M., Sutton G.G., Nierman W.C., Fouts D.E.;
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
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. {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:EMF98921.1}.
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DR   EMBL; AKWO02000078; EMF98921.1; -; Genomic_DNA.
DR   AlphaFoldDB; M3GDB3; -.
DR   BioCyc; LBOR1193007:G11KN-783-MONOMER; -.
DR   Proteomes; UP000011783; Unassembled WGS sequence.
DR   GO; GO:0046912; F:acyltransferase activity, acyl groups converted into alkyl on transfer; IEA:InterPro.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
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   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:ARBA00022605};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011783};
KW   Transferase {ECO:0000256|RuleBase:RU003523}.
FT   DOMAIN          9..110
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   110 AA;  12067 MW;  37EABCB52EC1EE9F CRC64;
     MATDQKDYVR IFDTTLRDGE QCPGAAMTEN EKLEIAAQLA AMKVDIIEAG FPISSPVQFQ
     AVERIARETE GPTIAALARA MKADIEAAFK ALQPAKKEEF IRSLLPLRST
//
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