ID LEUC_ECOSE Reviewed; 466 AA.
AC B6HZ52;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 29-MAY-2013, entry version 40.
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=ECSE_0072;
OS Escherichia coli (strain SE11).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=409438;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SE11;
RX PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H.,
RA Ooka T., Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT "Complete genome sequence and comparative analysis of the wild-type
RT commensal Escherichia coli strain SE11 isolated from a healthy
RT adult.";
RL DNA Res. 15:375-386(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 1 subfamily.
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DR EMBL; AP009240; BAG75596.1; -; Genomic_DNA.
DR RefSeq; YP_002291347.1; NC_011415.1.
DR ProteinModelPortal; B6HZ52; -.
DR SMR; B6HZ52; 4-457.
DR STRING; 409438.ECSE_0072; -.
DR PRIDE; B6HZ52; -.
DR EnsemblBacteria; BAG75596; BAG75596; ECSE_0072.
DR GeneID; 6998443; -.
DR KEGG; ecy:ECSE_0072; -.
DR PATRIC; 18418527; VBIEscCol83070_0191.
DR eggNOG; COG0065; -.
DR HOGENOM; HOG000226972; -.
DR KO; K01703; -.
DR OMA; DIRQGIV; -.
DR ProtClustDB; PRK05478; -.
DR BioCyc; ECOL409438:GHUU-72-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_01026; LeuC_type1; 1; -.
DR InterPro; IPR004430; 3-IsopropMal_deHydase_lsu.
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 PANTHER; PTHR11670; PTHR11670; 1.
DR Pfam; PF00330; Aconitase; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase_N; 1.
DR TIGRFAMs; TIGR00170; leuC; 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 1 466 3-isopropylmalate dehydratase large
FT subunit.
FT /FTId=PRO_1000135684.
FT METAL 347 347 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 407 407 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 410 410 Iron-sulfur (4Fe-4S) (By similarity).
SQ SEQUENCE 466 AA; 49882 MW; 2B225514207C5EFA CRC64;
MAKTLYEKLF DAHVVYEAEN ETPLLYIDRH LVHEVTSPQA FDGLRAHGRP VRQPGKTFAT
MDHNVSTQTK DINACGEMAR IQMQELIKNC KEFGVELYDL NHPYQGIVHV MGPEQGVTLP
GMTIVCGDSH TATHGAFGAL AFGIGTSEVE HVLATQTLKQ GRAKTMKIEV QGKAAPGITA
KDIVLAIIGK TGSAGGTGHV VEFCGEAIRD LSMEGRMTLC NMAIEMGAKA GLVAPDETTF
NYVKGRLHAP KGKDFDDAVA YWKTLQTDEG ATFDTVVTLQ AEEISPQVTW GTNPGQVISV
NDNIPDPASF ADPVERASAE KALAYMGLKP GIPLTEVAID KVFIGSCTNS RIEDLRAAAE
IAKGRKVAPG VQALVVPGSG PVKAQAEAEG LDKIFIEAGF EWRLPGCSMC LAMNNDRLNP
GERCASTSNR NFEGRQGRGG RTHLVSPAMA AAAAVTGHFA DIRNIK
//
