ID A4J182_DESRM Unreviewed; 418 AA.
AC A4J182;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 01-MAY-2013, entry version 45.
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=Dred_0286;
OS Desulfotomaculum reducens (strain MI-1).
OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC Desulfotomaculum.
OX NCBI_TaxID=349161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000612; ABO48835.1; -; Genomic_DNA.
DR RefSeq; YP_001111660.1; NC_009253.1.
DR ProteinModelPortal; A4J182; -.
DR STRING; 349161.Dred_0286; -.
DR EnsemblBacteria; ABO48835; ABO48835; Dred_0286.
DR GeneID; 4957291; -.
DR KEGG; drm:Dred_0286; -.
DR PATRIC; 21726376; VBIDesRed82656_0297.
DR eggNOG; COG0065; -.
DR HOGENOM; HOG000226971; -.
DR KO; K01703; -.
DR OMA; VIPFDHQ; -.
DR ProtClustDB; PRK00402; -.
DR BioCyc; DRED349161:GHP6-386-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 418 AA; 45174 MW; A6D72831ABF10DF8 CRC64;
MTITEKVLAA AAGKESVKPG ELINAKVDLV LANDITAPVA IKEFQKIGLD KVWDKNRVAL
VPDHFTPNKD IKSAEQAKLV RDFAHTQELA NYFEVGRMGI EHCLLPEQGL VGPGDVIIGA
DSHTCTYGAL GAFATGVGST DLAAAMALGE TWFKVPESIK FVFNGQLNKY VGGKDLILHT
IGQIGVDGAL YKAMEFCGEA ISQLSMDGRF TMCNMAIEAG GKNGIIQPDE ITRQYVEGRT
KRPYTFYTSD PDAQYSKVYE FDVNKIEPQV AFPHLPENAR PVSQAGHVDI DQAVIGSCTN
GRMEDLRLAA EILKGKKVHQ QVRLIVIPGT QEIYRQAMRE GLFEIFLDAG AVVSTPTCGP
CLGGHMGILA KGERCIATTN RNFVGRMGHA ESEVYLANPA VAAASAITGR ISHPQEVL
//
