ID LEUC_SALPK Reviewed; 466 AA.
AC B5BLB3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 01-MAY-2013, entry version 38.
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=SSPA0109;
OS Salmonella paratyphi A (strain AKU_12601).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=554290;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AKU_12601;
RA Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hassan R.,
RA Bhutta Z., Quail M., Norbertczak H., Danielle W., Simmonds M.,
RA White B., Bason N., Mungall K., Dougan G., Parkhill J.;
RT "Complete genome of a clinical isolate of Salmonella enterica serovar
RT Paratyphi A.";
RL Submitted (JUN-2008) 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 1 subfamily.
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DR EMBL; FM200053; CAR58220.1; -; Genomic_DNA.
DR RefSeq; YP_002140954.1; NC_011147.1.
DR ProteinModelPortal; B5BLB3; -.
DR STRING; 554290.SSPA0109; -.
DR PRIDE; B5BLB3; -.
DR EnsemblBacteria; CAR58220; CAR58220; SSPA0109.
DR GeneID; 6809387; -.
DR KEGG; sek:SSPA0109; -.
DR PATRIC; 32339711; VBISalEnt134303_0124.
DR eggNOG; COG0065; -.
DR HOGENOM; HOG000226972; -.
DR KO; K01703; -.
DR OMA; DIRQGIV; -.
DR ProtClustDB; PRK05478; -.
DR BioCyc; SENT554290:GJDA-112-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; -; 3.
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_1000135712.
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; 49736 MW; BC0B9C45B930C4B4 CRC64;
MAKTLYEKLF DAHVVFEAPN ETPLLYIDRH LVHEVTSPQA FDGLRAHHRP VRQPGKTFAT
MDHNVSTQTK DINASGEMAR IQMQELIKNC NEFGVELYDL NHPYQGIVHV MGPEQGVTLP
GMTIVCGDSH TATHGAFGAL AFGIGTSEVE HVLATQTLKQ GRAKTMKIEV TGSAAPGITA
KDIVLAIIGK TGSAGGTGHV VEFCGDAIRA LSMEGRMTLC NMAIEMGAKA GLVAPDETTF
NYVKGRLHAP KGCDFDEAVE YWKTLKTDDG ATFDTVVTLR AEEIAPQVTW GTNPGQVISV
TDIIPDPASF SDPVERASAE KALAYMGLQP GVPLTDVAID KVFIGSCTNS RIEDLRAAAE
VAKGRKVAPG VQALVVPGSG PVKAQAEAEG LDKIFIEAGF EWRLPGCSMC LAMNNDRLNP
GERCASTSNR NFEGRQGRGG RTHLVSPAMA AAAAVTGHFA DIRSIK
//
