ID   LEU1_METI4              Reviewed;         506 AA.
AC   B3DX88;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=Minf_1743;
OS   Methylacidiphilum infernorum (isolate V4) (Methylokorus infernorum (strain
OS   V4)).
OC   Bacteria; Verrucomicrobia; Methylacidiphilae; Methylacidiphilales;
OC   Methylacidiphilaceae; Methylacidiphilum.
OX   NCBI_TaxID=481448;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate V4;
RX   PubMed=18593465; DOI=10.1186/1745-6150-3-26;
RA   Hou S., Makarova K.S., Saw J.H., Senin P., Ly B.V., Zhou Z., Ren Y.,
RA   Wang J., Galperin M.Y., Omelchenko M.V., Wolf Y.I., Yutin N., Koonin E.V.,
RA   Stott M.B., Mountain B.W., Crowe M.A., Smirnova A.V., Dunfield P.F.,
RA   Feng L., Wang L., Alam M.;
RT   "Complete genome sequence of the extremely acidophilic methanotroph isolate
RT   V4, Methylacidiphilum infernorum, a representative of the bacterial phylum
RT   Verrucomicrobia.";
RL   Biol. Direct 3:26-26(2008).
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; CP000975; ACD83797.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3DX88; -.
DR   SMR; B3DX88; -.
DR   STRING; 481448.Minf_1743; -.
DR   EnsemblBacteria; ACD83797; ACD83797; Minf_1743.
DR   KEGG; min:Minf_1743; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_022158_0_1_0; -.
DR   OMA; NTMRMLV; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000009149; 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   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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Leucine biosynthesis; Transferase.
FT   CHAIN           1..506
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_1000149220"
FT   DOMAIN          8..272
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   506 AA;  55078 MW;  A5F395EA5051C9C8 CRC64;
     MEMTANRLIV FDTTLRDGEQ CPGASMTSRQ KLEVAKQLAR LGVDVIEAGF PVISQGDFES
     VSEIAAQVKG PKICGLARCL PKDIEAAAEA LKAAADAARI HVFLATSQIH RRFKLAKDEE
     EIVRIAVEGV RLAKRYVQDV EFSAEDASRT EPEFLAKIIQ KVIEAGATTV NIPDTVGYAV
     PEEFASLIRY LFDHVQDIDK VVVSVHCHND LGLAVSNSLA AIKAGARQVE GTINGIGERA
     GNAALEEIIM ALHTRPDAFG KIETGIQLKE ILRTSRLVSR MSGLAVQRNK AVVGENAFAH
     AAGIHQDGIL KKRETYEIID PKIIGWEQSE LPLTKHSGRA ALENRLKILG FELEKEEIDN
     IFSQFKQIGD KKKFIYDDDL VSLVEGQISR IKETYELEYV AVTVCSGGIP MATIKLRHGE
     EVLVDASTGD GAVDAAMKAV DRITGQHGHL VEYEVKSVTE GKDAIGEVTV KVNFDSKKLV
     TAKAASTDVI EASIKAYLNA VNKALL