LEU1_NEIMB
ID LEU1_NEIMB Reviewed; 517 AA.
AC Q9JZG1;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 114.
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}; OrderedLocusNames=NMB1070;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
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_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 -!- 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: Homotetramer. {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}.
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DR EMBL; AE002098; AAF41465.1; -; Genomic_DNA.
DR PIR; G81125; G81125.
DR RefSeq; NP_274103.1; NC_003112.2.
DR PDB; 3RMJ; X-ray; 1.95 A; A/B=1-364.
DR PDBsum; 3RMJ; -.
DR AlphaFoldDB; Q9JZG1; -.
DR SMR; Q9JZG1; -.
DR STRING; 122586.NMB1070; -.
DR PaxDb; Q9JZG1; -.
DR EnsemblBacteria; AAF41465; AAF41465; NMB1070.
DR KEGG; nme:NMB1070; -.
DR PATRIC; fig|122586.8.peg.1361; -.
DR HOGENOM; CLU_022158_0_1_4; -.
DR OMA; NTMRMLV; -.
DR BRENDA; 2.3.3.13; 3593.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IBA:GO_Central.
DR GO; GO:0009098; P:leucine biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.30.160.270; -; 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 Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF08502; LeuA_dimer; 1.
DR SMART; SM00917; LeuA_dimer; 1.
DR SUPFAM; SSF110921; SSF110921; 1.
DR TIGRFAMs; TIGR00973; leuA_bact; 1.
DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; Leucine biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..517
FT /note="2-isopropylmalate synthase"
FT /id="PRO_0000140364"
FT DOMAIN 7..269
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:3RMJ"
FT HELIX 13..17
FT /evidence="ECO:0007829|PDB:3RMJ"
FT HELIX 27..40
FT /evidence="ECO:0007829|PDB:3RMJ"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:3RMJ"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:3RMJ"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:3RMJ"
FT STRAND 68..79
FT /evidence="ECO:0007829|PDB:3RMJ"
FT HELIX 80..90
FT /evidence="ECO:0007829|PDB:3RMJ"
FT STRAND 93..103
FT /evidence="ECO:0007829|PDB:3RMJ"
FT HELIX 106..111
FT /evidence="ECO:0007829|PDB:3RMJ"
FT HELIX 117..131
FT /evidence="ECO:0007829|PDB:3RMJ"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:3RMJ"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:3RMJ"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:3RMJ"
FT HELIX 150..163
FT /evidence="ECO:0007829|PDB:3RMJ"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:3RMJ"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:3RMJ"
FT HELIX 179..192
FT /evidence="ECO:0007829|PDB:3RMJ"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:3RMJ"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:3RMJ"
FT HELIX 212..221
FT /evidence="ECO:0007829|PDB:3RMJ"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:3RMJ"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:3RMJ"
FT HELIX 243..252
FT /evidence="ECO:0007829|PDB:3RMJ"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:3RMJ"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:3RMJ"
FT HELIX 268..279
FT /evidence="ECO:0007829|PDB:3RMJ"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:3RMJ"
FT TURN 292..295
FT /evidence="ECO:0007829|PDB:3RMJ"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:3RMJ"
SQ SEQUENCE 517 AA; 55397 MW; 6D9EF77D2F6FCD6A CRC64;
MTQTNRVIIF DTTLRDGEQS PGAAMTKEEK IRVARQLEKL GVDIIEAGFA AASPGDFEAV
NAIAKTITKS TVCSLSRAIE RDIRQAGEAV APAPKKRIHT FIATSPIHME YKLKMKPKQV
IEAAVKAVKI AREYTDDVEF SCEDALRSEI DFLAEICGAV IEAGATTINI PDTVGYSIPY
KTEEFFRELI AKTPNGGKVV WSAHCHNDLG LAVANSLAAL KGGARQVECT VNGLGERAGN
ASVEEIVMAL KVRHDLFGLE TGIDTTQIVP SSKLVSTITG YPVQPNKAIV GANAFSHESG
IHQDGVLKHR ETYEIMSAES VGWATNRLSL GKLSGRNAFK TKLADLGIEL ESEEALNAAF
ARFKELADKK REIFDEDLHA LVSDEMGSMN AESYKFISQK ISTETGEEPR ADIVFSIKGE
EKRASATGSG PVDAIFKAIE SVAQSGAALQ IYSVNAVTQG TESQGETSVR LARGNRVVNG
QGADTDVLVA TAKAYLSALS KLEFSAAKPK AQGSGTI
