ID LEUC_CLOK5 Reviewed; 420 AA.
AC A5MZ75;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 01-MAY-2013, entry version 53.
DE RecName: Full=3-isopropylmalate dehydratase large subunit;
DE EC=4.2.1.33;
DE AltName: Full=Alpha-IPM isomerase;
DE Short=IPMI;
DE AltName: Full=Isopropylmalate isomerase;
GN Name=leuC; OrderedLocusNames=CKL_2159;
OS Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=431943;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680;
RX PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA Hagemeier C., Thauer R.K., Gottschalk G.;
RT "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT metabolic features.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
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; CP000673; EDK34171.1; -; Genomic_DNA.
DR RefSeq; YP_001395542.1; NC_009706.1.
DR ProteinModelPortal; A5MZ75; -.
DR STRING; 431943.CKL_2159; -.
DR EnsemblBacteria; EDK34171; EDK34171; CKL_2159.
DR GeneID; 5394027; -.
DR KEGG; ckl:CKL_2159; -.
DR PATRIC; 19465827; VBICloKlu111549_2248.
DR eggNOG; COG0065; -.
DR HOGENOM; HOG000226971; -.
DR KO; K01703; -.
DR OMA; VIPFDHQ; -.
DR ProtClustDB; PRK00402; -.
DR BioCyc; CKLU431943:GJF1-2152-MONOMER; -.
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; Complete proteome; Iron;
KW Iron-sulfur; Leucine biosynthesis; Lyase; Metal-binding.
FT CHAIN 1 420 3-isopropylmalate dehydratase large
FT subunit.
FT /FTId=PRO_1000084236.
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 420 AA; 45013 MW; 51EB2A80B4C79DDA CRC64;
MAMTMTQKIL ASHAGLDSVK SGELIKVKLD LVLGNDITTP VAINEFNKIG SNKVFHKEKV
AIVPDHFTPN KDIKSAEQCK CVREFAKDKD IKNYFEIGQM GIEHALIPEK GLAVCGDVII
GADSHTCTYG ALGAFSTGVG STDMAAGMAT GEAWFKVPEA IKFVLNGKLS PWVSGKDIIL
HIIGMIGVDG ALYNSMEFTG EGVGELSMDD RFTIANMAIE AGAKNGIFPV DEKTIEYVKE
HSNRSYTVYE ADEDAEYVKT IEIDLSKIPP TVAFPHIPEN TRTIDEVGEI KIDQVVIGSC
TNGRIGDLRV AAKVLKGRKV NSNVRTIIFP ATQSIYLQAM KEGLLEIFIE SGAVVSTPTC
GPCLGGHMGI LAKGERAVAT TNRNFTGRMG HVESEVYLAS PAVAAASAVT GKISSPEEVV
//
