GenomeNet

Database: UniProt/TrEMBL
Entry: C0R088_BRAHW
LinkDB: C0R088_BRAHW
Original site: C0R088_BRAHW 
ID   C0R088_BRAHW            Unreviewed;       415 AA.
AC   C0R088;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   01-MAY-2013, entry version 32.
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; OrderedLocusNames=BHWA1_01043;
OS   Brachyspira hyodysenteriae (strain ATCC 49526 / WA1).
OC   Bacteria; Spirochaetes; Spirochaetales; Brachyspiraceae; Brachyspira.
OX   NCBI_TaxID=565034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49526 / WA1;
RX   PubMed=19262690; DOI=10.1371/journal.pone.0004641;
RA   Bellgard M.I., Wanchanthuek P., La T., Ryan K., Moolhuijzen P.,
RA   Albertyn Z., Shaban B., Motro Y., Dunn D.S., Schibeci D., Hunter A.,
RA   Barrero R., Phillips N.D., Hampson D.J.;
RT   "Genome sequence of the pathogenic intestinal spirochete brachyspira
RT   hyodysenteriae reveals adaptations to its lifestyle in the porcine
RT   large intestine.";
RL   PLoS ONE 4:e4641-e4641(2009).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001357; ACN83526.1; -; Genomic_DNA.
DR   RefSeq; YP_002721230.1; NC_012225.1.
DR   STRING; 565034.BHWA1_01043; -.
DR   EnsemblBacteria; ACN83526; ACN83526; BHWA1_01043.
DR   GeneID; 7666144; -.
DR   KEGG; bhy:BHWA1_01043; -.
DR   PATRIC; 21180173; VBIBraHyo62857_1024.
DR   eggNOG; COG0065; -.
DR   HOGENOM; HOG000226971; -.
DR   KO; K01703; -.
DR   OMA; VIPFDHQ; -.
DR   ProtClustDB; PRK00402; -.
DR   BioCyc; BHYO565034:GJI7-1038-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   METAL       298    298       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       358    358       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       361    361       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   415 AA;  44758 MW;  AE522FB7B34D20CB CRC64;
     MTITQKILAA HAGVEKVEAG ELIMVKTDLV LGNDITSPVA INEFEKYGFD KVFDKEKIAL
     VMDHFAPNKD IKAAEQCKQC RDFANKYDIS NYYDVGDMGV EHALLPEKGL VAPGEVIIGA
     DSHTCTYGAF GAFSTGVGST DMAAAMATGQ VWFKVPSAIK FNLKGKLKPN VSGKDVILHI
     IGMIGVDGAL YKSMEFRGEG VSSLTMDDRA CIANMAIEAG AKNGIFEVDD QTIEYLKDIV
     KRDYTVFKAD DDAVYDKEYD IDLSLIEPTV ACPHLPENTK EAKELKNIKV DQVVIGSCTN
     GRLSDMATAA NILKGKKVAK GVRCIVIPAT QKVYKECIKL GYMDIFIDAG CAVSTPTCGP
     CLGGYMGILA HDEVAVTTTN RNFVGRMGDK TSKVYLASPA TAAYSAITGY ITEPK
//
DBGET integrated database retrieval system