ID   A0FDI2_LEPIR            Unreviewed;       431 AA.
AC   A0FDI2;
DT   28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2006, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Citramalate synthase {ECO:0000313|EMBL:ABK13751.1};
DE   Flags: Fragment;
GN   Name=cimA {ECO:0000313|EMBL:ABK13751.1};
OS   Leptospira interrogans serovar Pyrogenes.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=280500 {ECO:0000313|EMBL:ABK13751.1};
RN   [1] {ECO:0000313|EMBL:ABK13751.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=4 {ECO:0000313|EMBL:ABK13751.1};
RA   Zou Y., Guo X., Picardeau M., Xu H., Zhao G.;
RT   "A comprehensive survey on isoleucine biosynthesis pathways in seven
RT   epidemic Leptospira interrogans reference strains of China.";
RL   FEMS Microbiol. Ecol. 269:90-96(2007).
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DR   EMBL; DQ978315; ABK13751.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0FDI2; -.
DR   BRENDA; 4.1.3.22; 2986.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:InterPro.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.160.740; -; 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; IPR036230; LeuA_allosteric_dom_sf.
DR   InterPro; IPR000891; PYR_CT.
DR   PANTHER; PTHR10277:SF57; (R)-CITRAMALATE SYNTHASE CIMA; 1.
DR   PANTHER; PTHR10277; HOMOCITRATE SYNTHASE-RELATED; 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   PROSITE; PS50991; PYR_CT; 1.
PE   4: Predicted;
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|ARBA:ARBA00022679}.
FT   DOMAIN          1..241
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABK13751.1"
FT   NON_TER         431
FT                   /evidence="ECO:0000313|EMBL:ABK13751.1"
SQ   SEQUENCE   431 AA;  47831 MW;  C874DDBBAB85A9A9 CRC64;
     FRELNIAKFL LQKLNVDRVE IASARVSKGE LETVQKIMEW AATEQLTERI EILGFVDGNK
     TVDWIKDSGA KVLNLLTKGS LHHLEKQLGK TPKEFFTDVS FVIEYAIKSG LKINVYLEDW
     SNGFRNSPDY VKSLVEHLSK EHIERIFLPD TLGVLSPEET FQGVDSLIQK YPDIHFEFHG
     HNDYDLSVAN SLQAIRAGVK GLHASINGLG ERAGNTPLEA LVTTIHDKSN SKTNINEIAI
     TEASRLVEVF SGKRISANRP IVGEDVFTQT AGVHADGDKK GNLYANPILP ERFGRKRSYA
     LGKLAGKASI SENVKQLGMV LSDVVLQKVL ERVIELGDQN KLVTPEDLPF IIADVSGRTG
     EKVLTIKSCN IHSGIGIRPH AQIELEYQGK IHKEISEGDG GYDAFMNALT KITNRLGISI
     PKLIDYEVRI L
//