ID LEUC_CLOD6 Reviewed; 425 AA.
AC Q18AJ2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 01-MAY-2013, entry version 62.
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=CD630_09900;
OS Clostridium difficile (strain 630).
OC Bacteria; Firmicutes; Clostridia; Clostridiales;
OC Peptostreptococcaceae.
OX NCBI_TaxID=272563;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630;
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K.,
RA Unwin L., Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a
RT highly mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(2006).
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; AM180355; CAJ67831.1; -; Genomic_DNA.
DR RefSeq; YP_001087471.1; NC_009089.1.
DR ProteinModelPortal; Q18AJ2; -.
DR STRING; 272563.CD0990; -.
DR EnsemblBacteria; CAJ67831; CAJ67831; CD630_09900.
DR GeneID; 4914340; -.
DR KEGG; cdf:CD630_09900; -.
DR PATRIC; 19440297; VBICloDif38397_1041.
DR eggNOG; COG0065; -.
DR HOGENOM; HOG000226971; -.
DR KO; K01703; -.
DR OMA; VIPFDHQ; -.
DR ProtClustDB; CLSK2534650; -.
DR BioCyc; CDIF272563:GJFE-1137-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 1 425 3-isopropylmalate dehydratase large
FT subunit.
FT /FTId=PRO_1000063643.
FT METAL 305 305 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 365 365 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 368 368 Iron-sulfur (4Fe-4S) (By similarity).
SQ SEQUENCE 425 AA; 45849 MW; B6CC456152B7C7DA CRC64;
MGMTMTQKIL AKHAKLNEVK KGQLIEADLD VVLGNDITSP VAIREFEKLG IEDVYDKTKV
VMVLDHFTPN KDIKSAEQCK FTRSFAKSKG VVNFFDVGDM GIEHVLLPEK GIVTAGDVII
GADSHTCTYG ALGAFSTGVG STDMGAGMAT GKCWFKVPGA IKFVLKNKPN KWISGKDIIL
HIIGEIGVDG ALYKSMEFCG DGVEYLSMDD RFTICNMAIE AGAKNGIFPV DDKTMEYINS
HKCSTMTKDV NIYEADEDAV YDEVYEIDLA KLKETVAFPH LPENTRTVDE IDKDIKIDQV
VIGSCTNGRI SDLEVVAEIM KGKKVADGVR VMIFPGTQKV YLEAIEKGYI TTFIEAGAAV
STPTCGPCLG GHMGILAAGE KSISTTNRNF VGRMGHVDSE VYLASPAVAA ASAITGKISK
PSEII
//
