ID LEU1_XANCB Reviewed; 520 AA. AC B0RP28; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 82. DE RecName: Full=2-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_01025}; DE EC=2.3.3.13 {ECO:0000255|HAMAP-Rule:MF_01025}; DE AltName: Full=Alpha-IPM synthase {ECO:0000255|HAMAP-Rule:MF_01025}; DE AltName: Full=Alpha-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_01025}; GN Name=leuA {ECO:0000255|HAMAP-Rule:MF_01025}; GN OrderedLocusNames=xcc-b100_0870; OS Xanthomonas campestris pv. campestris (strain B100). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=509169; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B100; RX PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013; RA Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T., RA Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K., RA Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K., RA Puehler A.; RT "The genome of Xanthomonas campestris pv. campestris B100 and its use for RT the reconstruction of metabolic pathways involved in xanthan RT biosynthesis."; RL J. Biotechnol. 134:33-45(2008). CC -!- FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA CC with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3- CC hydroxy-4-methylpentanoate (2-isopropylmalate). {ECO:0000255|HAMAP- CC Rule:MF_01025}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2- CC isopropylmalate + CoA + H(+); Xref=Rhea:RHEA:21524, ChEBI:CHEBI:1178, CC ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.13; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01025}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01025}; CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine CC from 3-methyl-2-oxobutanoate: step 1/4. {ECO:0000255|HAMAP- CC Rule:MF_01025}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01025}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01025}. CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase CC family. LeuA type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01025}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AM920689; CAP50213.1; -; Genomic_DNA. DR AlphaFoldDB; B0RP28; -. DR SMR; B0RP28; -. DR KEGG; xca:xcc-b100_0870; -. DR HOGENOM; CLU_022158_0_1_6; -. DR UniPathway; UPA00048; UER00070. DR Proteomes; UP000001188; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd07940; DRE_TIM_IPMS; 1. DR Gene3D; 1.10.238.260; -; 1. DR Gene3D; 3.30.160.270; -; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR HAMAP; MF_01025; LeuA_type1; 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; IPR005671; LeuA_bact_synth. DR InterPro; IPR000891; PYR_CT. DR NCBIfam; TIGR00973; leuA_bact; 1. 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; Branched-chain amino acid biosynthesis; Cytoplasm; KW Leucine biosynthesis; Manganese; Metal-binding; Transferase. FT CHAIN 1..520 FT /note="2-isopropylmalate synthase" FT /id="PRO_1000149334" FT DOMAIN 12..274 FT /note="Pyruvate carboxyltransferase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01025" FT REGION 396..520 FT /note="Regulatory domain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01025" FT BINDING 21 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01025" FT BINDING 209 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01025" FT BINDING 211 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01025" FT BINDING 245 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01025" SQ SEQUENCE 520 AA; 56222 MW; A8879B31E2E509D9 CRC64; MNTTVSNQTP HIRIFDTTLR DGEQSPGCSM TPQQKLVMAR ALDALGVDII ETGFPASSYS DREAVAMMGR ELRRPTLAVL SRCLQADIEI SARALEAAAN PRLHVFLSTS PLHREHKLRM SREQVLESVH KHVTLARGYI DDIEFSAEDA TRTEEDFLAE VTRVAIAAGA TTINLPDTVG FTTPEEIRGM FSRLIASVEG AEKVIFSTHC HNDLGLAAAN SLAAIEGGAR QVECTINGIG ERAGNCALEE ITMALKVRGA FYNLDTAINT PRIVSTSQLL QRLVGMPVQR NKAVVGGNAF AHESGIHQHG MLRHRGTYEI MRPEDVGWES SQMVLGRHSG RAAVEQRLRA LGYLLEEDEA KLVFEQFKAL CEKQRVVTDA DLQALMQDAT VQEGYRLASM TISDVGSRAN ALVELSDPDG NRVAETAQGN GPVDALFGAL ASATGVKLEL DSYQVHSVGI GADARGEASL SVRHDGVEYE GTGTSKDIIE ASALAWLDVA NRLLRQRERG VVAGKTAAVA //