LEU12_BACP2
ID LEU12_BACP2 Reviewed; 553 AA.
AC A8FAK7;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=2-isopropylmalate synthase 2 {ECO:0000255|HAMAP-Rule:MF_00572};
DE EC=2.3.3.13 {ECO:0000255|HAMAP-Rule:MF_00572};
DE AltName: Full=Alpha-IPM synthase 2 {ECO:0000255|HAMAP-Rule:MF_00572};
DE AltName: Full=Alpha-isopropylmalate synthase 2 {ECO:0000255|HAMAP-Rule:MF_00572};
GN Name=leuA2 {ECO:0000255|HAMAP-Rule:MF_00572}; OrderedLocusNames=BPUM_0582;
OS Bacillus pumilus (strain SAFR-032).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=315750;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAFR-032;
RX PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA Weinstock G.M.;
RT "Paradoxical DNA repair and peroxide resistance gene conservation in
RT Bacillus pumilus SAFR-032.";
RL PLoS ONE 2:E928-E928(2007).
CC -!- FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA
CC with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-
CC hydroxy-4-methylpentanoate (2-isopropylmalate). {ECO:0000255|HAMAP-
CC Rule:MF_00572}.
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_00572};
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_00572}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00572}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00572}.
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DR EMBL; CP000813; ABV61274.1; -; Genomic_DNA.
DR RefSeq; WP_012009125.1; NZ_VEIA01000005.1.
DR AlphaFoldDB; A8FAK7; -.
DR SMR; A8FAK7; -.
DR STRING; 315750.BPUM_0582; -.
DR EnsemblBacteria; ABV61274; ABV61274; BPUM_0582.
DR KEGG; bpu:BPUM_0582; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_004588_3_2_9; -.
DR OMA; WPDKVID; -.
DR OrthoDB; 840579at2; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000001355; Chromosome.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd07942; DRE_TIM_LeuA; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.30.160.270; -; 1.
DR HAMAP; MF_00572; LeuA_type2; 1.
DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005668; IPM_Synthase.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR039371; LeuA_N_DRE-TIM.
DR InterPro; IPR000891; PYR_CT.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF08502; LeuA_dimer; 1.
DR SMART; SM00917; LeuA_dimer; 1.
DR SUPFAM; SSF110921; SSF110921; 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;
KW Leucine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..553
FT /note="2-isopropylmalate synthase 2"
FT /id="PRO_0000406870"
FT DOMAIN 31..304
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 553 AA; 63211 MW; DBA1F2B00E52DDF2 CRC64;
MFNHKKYEKK YFLPPNLTYD WVKNETLESA PIWCSVDLRD GNQALPIPMN LEEKLEMFQL
LVEIGFKEIE IAFPAASDTE FRLLRTLIDH HMIPDDVTIM VITQAREHII RRTFEAIKGV
PKAIVHLYNS TSEAQRRQVF KKTKDEVKQM AMDGAILVKE LAEKTESDIY FQYSPESFPG
TEVDYALDIC NSVLDIWKPT PNHKAIINIP TTVEYSMPHI FASQIEYIHK NLSYRDSVTL
SVHPHNDRGS GVSDAEFGVL AGAERVEGTL FGIGERTGNV DLITLAMNMY SQGYDPKLNF
NNLEAIRKQY EKLTNITVHE RQPYSGEMVF TAFSGSHQDA ISKGMKYRKE HHVDKWDVPY
IPVDPVDLGR NYQTDVIRIN SQSGKGGIGY ILETNYGIQL PYQMNEAMGY EAKKVSDQSN
RELSVEEIYH VFEKQYVDFH PHFQLLDYQF HKGEKQEVTL TLLRDHQQID IQGTGTGSLD
AISNALKAYF HLEYDLEVYE QNSLGKDSQA KACAQIGISH QGKMHWGAGI DKDIIEATVK
ALVVAVNRLE VWM
