ID H2JFQ0_9CLOT Unreviewed; 419 AA.
AC H2JFQ0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 06-MAR-2013, entry version 10.
DE RecName: Full=3-isopropylmalate dehydratase large subunit;
DE EC=4.2.1.33;
DE AltName: Full=Alpha-IPM isomerase;
DE AltName: Full=Isopropylmalate isomerase;
GN Name=leuC; ORFNames=Clo1100_0122;
OS Clostridium sp. BNL1100.
OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=755731;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BNL1100;
RX PubMed=23209234; DOI=10.1128/JB.01908-12;
RA Li L.L., Taghavi S., Izquierdo J.A., van der Lelie D.;
RT "Complete Genome Sequence of Clostridium sp. Strain BNL1100, a
RT Cellulolytic Mesophile Isolated from Corn Stover.";
RL J. Bacteriol. 194:6982-6983(2012).
CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate
CC and 3-isopropylmalate, via the formation of 2-isopropylmaleate (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate = (2S)-2-
CC isopropylmalate.
CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity).
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC leucine from 3-methyl-2-oxobutanoate: step 2/4.
CC -!- SUBUNIT: Heterodimer of LeuC and LeuD (By similarity).
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC
CC type 2 subfamily.
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DR EMBL; CP003259; AEY64414.1; -; Genomic_DNA.
DR RefSeq; YP_005146219.1; NC_016791.1.
DR GeneID; 11723486; -.
DR KEGG; clb:Clo1100_0122; -.
DR KO; K01703; -.
DR UniPathway; UPA00048; UER00071.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:HAMAP.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:HAMAP.
DR Gene3D; 3.30.499.10; -; 2.
DR Gene3D; 3.40.1060.10; -; 1.
DR HAMAP; MF_01027; LeuC_type2; 1; -.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR015937; Acoase/IPM_deHydtase.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR015932; Aconitase/IPMdHydase_lsu_aba_2.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR011826; HAcnase/IPMdehydase_lsu_prok.
DR InterPro; IPR006251; Homoacnase/IPMdehydase_lsu.
DR InterPro; IPR011823; IsopropMal_deHydtase_lsu_bac.
DR PANTHER; PTHR11670; PTHR11670; 1.
DR PANTHER; PTHR11670:SF6; PTHR11670:SF6; 1.
DR Pfam; PF00330; Aconitase; 2.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase_N; 1.
DR TIGRFAMs; TIGR01343; hacA_fam; 1.
DR TIGRFAMs; TIGR02086; IPMI_arch; 1.
DR TIGRFAMs; TIGR02083; LEU2; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; Iron; Iron-sulfur;
KW Leucine biosynthesis; Lyase; Metal-binding.
FT METAL 300 300 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 360 360 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 363 363 Iron-sulfur (4Fe-4S) (By similarity).
SQ SEQUENCE 419 AA; 45024 MW; D7785CEC055A26C8 CRC64;
MGMTMTQKIL ANHAGADKVV PGQLIKAKLD MVLGNDITSP VAIKEFDKIG LDKVFDKNKI
AIVPDHFTPN KDIKSAEQVK VCREFSKRME IVNFFEVGQM GVEHALLPEK GLVVPGDVVI
GADSHTCTYG ALGAFSTGIG STDMAAGMAT GEAWFKVPEA IKFVLKGKPQ KWVGGKDVIL
HIIGMIGVDG ALYKSMEFTG DGVNALSMDD RFSMANMAIE AGAKNGIFEV DEKTVEYVKE
HSIRSYSIYK ADEDAEYSEV YEIDLAEIKP TVAFPHLPEN ARTIDKVGDI KIDQVVIGSC
TNGRIEDMRI AAEVLKGKKV SDNVRCIIIP ATQKIWKQAM NEGLFDIFID SGAAVSTPTC
GPCLGGHMGI LAKGERAVAT TNRNFVGRMG HPESEVYLAS PAVAAASAIA GRIAGPDEI
//
