ID I0XTY6_9LEPT Unreviewed; 432 AA.
AC I0XTY6;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN ORFNames=LEP1GSC185_2078 {ECO:0000313|EMBL:EIE02344.1};
OS Leptospira licerasiae serovar Varillal str. VAR 010.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1049972 {ECO:0000313|EMBL:EIE02344.1, ECO:0000313|Proteomes:UP000004889};
RN [1] {ECO:0000313|EMBL:EIE02344.1, ECO:0000313|Proteomes:UP000004889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VAR 010 {ECO:0000313|EMBL:EIE02344.1};
RX PubMed=23145189; DOI=10.1371/journal.pntd.0001853;
RA Ricaldi J.N., Fouts D.E., Selengut J.D., Harkins D.M., Patra K.P.,
RA Moreno A., Lehmann J.S., Purushe J., Sanka R., Torres M., Webster N.J.,
RA Vinetz J.M., Matthias M.A.;
RT "Whole Genome Analysis of Leptospira licerasiae Provides Insight into
RT Leptospiral Evolution and Pathogenicity.";
RL PLoS Negl. Trop. Dis. 6:E1853-E1853(2012).
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:EIE02344.1}.
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DR EMBL; AHOO02000005; EIE02344.1; -; Genomic_DNA.
DR AlphaFoldDB; I0XTY6; -.
DR PATRIC; fig|1049972.3.peg.1411; -.
DR OrthoDB; 9804858at2; -.
DR Proteomes; UP000004889; 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; 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 Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Transferase {ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 33..295
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 432 AA; 47234 MW; 315135DF71896E22 CRC64;
MEQKSNAISA TQYPSIQEMI IPGQGLKTPP VSPFFMDVTL RDGNQALRKP WNLEEKEIIF
KRLVKLGVQG IEVGFASASK QDFEACSYLA SLAPENIAIS SLSRAVEKEI DLSWEAIKKA
PRPRIHIVYP ISDFTIRNVL GISEKEVKEN IIRSVSYARK LAGNYGEVQF SGEHFGDSLE
NMDFAVEAFQ VALEAGADVV NLPNTVERYR PYLFVAMVRK VADSLPQGSK ISVHTHNDLG
MATATTVESF FAGATQLETA LNGLGERAGN TNTYEVAIAL HNCGVKVNLD LQTIYETSRI
VSRMSGVPIP EKAPLIGEDV VAHRSGIHQD GVSKTKDMKK GAYRAFDADL IGRPEGDRIA
FTSQSGKSAI YEILMQSGIS VSKEEASKLQ PILKSISENS GGGELSIEEI KDELGKLRSI
SKPSVRKKIS VD
//
