ID F7UVT2_EEGSY Unreviewed; 422 AA.
AC F7UVT2;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 29-MAY-2013, entry version 14.
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=EGYY_22220;
OS Eggerthella sp. (strain YY7918).
OC Bacteria; Actinobacteria; Coriobacteridae; Coriobacteriales;
OC Coriobacterineae; Coriobacteriaceae; Eggerthella.
OX NCBI_TaxID=502558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YY7918;
RA Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.;
RT "Complete genome sequence of the equol-producing bacterium Eggerthella
RT sp. strain YY7918 isolated from adult human intestine.";
RL Submitted (JUN-2011) 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.
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DR EMBL; AP012211; BAK45305.1; -; Genomic_DNA.
DR RefSeq; YP_004711706.1; NC_015738.1.
DR EnsemblBacteria; BAK45305; BAK45305; EGYY_22220.
DR GeneID; 10928955; -.
DR KEGG; eyy:EGYY_22220; -.
DR KO; K01703; -.
DR BioCyc; ESP502558:GI1S-2059-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.
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 302 302 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 362 362 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 365 365 Iron-sulfur (4Fe-4S) (By similarity).
SQ SEQUENCE 422 AA; 45030 MW; 438CD03618FA3291 CRC64;
MPRPMTMAEK ILAAHAGLDE VEPGQLIECD LDLVLSNDVT APIAVKEFRK IGVEKVFDPT
KIALVPDHYV PNKDIKSAEQ AKIVRDFARE QGITHYYEVG CMGVEHALLP EQGVVGAGDL
IIGADSHTCT YGALGAFATG VGSTDAGVGY ATGKAWFKVP ESLLFKIEGE LAPGVTGKDV
ILHIIGMIGV DGALYQAMEF TGSAIKNMDM DERMSISNMA IEAGGKAGLI EVDDVTRAYM
DGRVERPYTE YHSDPDAVYA KVYEIDAASI QPTVAFPHLP SNTRPAAEAR DVKIDQAVIG
SCTNGRIADM RQAAEVLRGR KIHPDVRCIV IPATQQVYRQ CMEEGLMDVF LDANCAVSTP
TCGPCLGGYM GILAAGERAI ATTNRNFVGR MGDPTSEVYL SSPAVAAASA VLGHIGLPED
LD
//
