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 01-MAY-2013, entry version 41.
DE RecName: Full=2-isopropylmalate synthase;
DE EC=2.3.3.13;
DE AltName: Full=Alpha-IPM synthase;
DE AltName: Full=Alpha-isopropylmalate synthase;
GN Name=leuA; OrderedLocusNames=Minf_1743;
OS Methylacidiphilum infernorum (isolate V4) (Methylokorus infernorum
OS (strain V4)).
OC Bacteria; Verrucomicrobia; unclassified Verrucomicrobia;
OC Methylacidiphilales; 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.,
RA Koonin E.V., Stott M.B., Mountain B.W., Crowe M.A., Smirnova A.V.,
RA Dunfield P.F., Feng L., Wang L., Alam M.;
RT "Complete genome sequence of the extremely acidophilic methanotroph
RT isolate V4, Methylacidiphilum infernorum, a representative of the
RT bacterial phylum Verrucomicrobia.";
RL Biol. Direct 3:26-26(2008).
CC -!- FUNCTION: Catalyzes the condensation of the acetyl group of
CC acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form
CC 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate) (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + 3-methyl-2-oxobutanoate + H(2)O =
CC (2S)-2-isopropylmalate + CoA.
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC leucine from 3-methyl-2-oxobutanoate: step 1/4.
CC -!- SUBUNIT: Homotetramer (By similarity).
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 1 subfamily.
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DR EMBL; CP000975; ACD83797.1; -; Genomic_DNA.
DR RefSeq; YP_001940395.1; NC_010794.1.
DR ProteinModelPortal; B3DX88; -.
DR STRING; 481448.Minf_1743; -.
DR EnsemblBacteria; ACD83797; ACD83797; Minf_1743.
DR GeneID; 6352689; -.
DR KEGG; min:Minf_1743; -.
DR PATRIC; 22492663; VBIMetInf111569_1807.
DR eggNOG; COG0119; -.
DR HOGENOM; HOG000046859; -.
DR KO; K01649; -.
DR OMA; VWSVHCH; -.
DR ProtClustDB; CLSK2337780; -.
DR BioCyc; MINF481448:GJEI-1780-MONOMER; -.
DR UniPathway; UPA00048; UER00070.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:HAMAP.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:HAMAP.
DR Gene3D; 3.20.20.70; -; 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; 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; 2-isopropylmalate_synth_dimer; 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 Complete proteome; Leucine biosynthesis; Transferase.
FT CHAIN 1 506 2-isopropylmalate synthase.
FT /FTId=PRO_1000149220.
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
//