LEUC_ECOLI
ID LEUC_ECOLI Reviewed; 466 AA.
AC P0A6A6; P30127; P78042; Q8FL77;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=3-isopropylmalate dehydratase large subunit {ECO:0000255|HAMAP-Rule:MF_01026};
DE EC=4.2.1.33 {ECO:0000255|HAMAP-Rule:MF_01026};
DE AltName: Full=Alpha-IPM isomerase {ECO:0000255|HAMAP-Rule:MF_01026};
DE Short=IPMI {ECO:0000255|HAMAP-Rule:MF_01026};
DE AltName: Full=Isopropylmalate isomerase {ECO:0000255|HAMAP-Rule:MF_01026};
GN Name=leuC {ECO:0000255|HAMAP-Rule:MF_01026};
GN OrderedLocusNames=b0072, JW0071;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2124684; DOI=10.1093/nar/18.23.7185;
RA Rosenthal E.R., Calvo J.M.;
RT "Aphidicolin inhibits DNA polymerase II of Escherichia coli, an alpha-like
RT DNA polymerase.";
RL Nucleic Acids Res. 18:7185-7186(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO 70
RP AND 361.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-205.
RC STRAIN=K12;
RX PubMed=8119295; DOI=10.1111/j.1432-1033.1994.tb18623.x;
RA Kirino H., Aoki M., Aoshima M., Hayashi Y., Ohba M., Yamagishi A.,
RA Wakagi T., Oshima T.;
RT "Hydrophobic interaction at the subunit interface contributes to the
RT thermostability of 3-isopropylmalate dehydrogenase from an extreme
RT thermophile, Thermus thermophilus.";
RL Eur. J. Biochem. 220:275-281(1994).
RN [6]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP PROTEIN SEQUENCE OF 2-5.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9740056; DOI=10.1002/elps.1150191114;
RA Tonella L., Walsh B.J., Sanchez J.-C., Ou K., Wilkins M.R., Tyler M.,
RA Frutiger S., Gooley A.A., Pescaru I., Appel R.D., Yan J.X., Bairoch A.,
RA Hoogland C., Morch F.S., Hughes G.J., Williams K.L., Hochstrasser D.F.;
RT "'98 Escherichia coli SWISS-2DPAGE database update.";
RL Electrophoresis 19:1960-1971(1998).
RN [8]
RP PROTEIN SEQUENCE OF 2-5.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC isopropylmalate, via the formation of 2-isopropylmaleate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate;
CC Xref=Rhea:RHEA:32287, ChEBI:CHEBI:1178, ChEBI:CHEBI:35121;
CC EC=4.2.1.33; Evidence={ECO:0000255|HAMAP-Rule:MF_01026};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01026};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01026};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 2/4. {ECO:0000255|HAMAP-
CC Rule:MF_01026}.
CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000255|HAMAP-
CC Rule:MF_01026}.
CC -!- INTERACTION:
CC P0A6A6; P30126: leuD; NbExp=4; IntAct=EBI-1113576, EBI-1113528;
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01026}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U00096; AAC73183.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96641.2; -; Genomic_DNA.
DR EMBL; D17631; BAA21004.1; -; Genomic_DNA.
DR EMBL; D17632; BAA21005.1; -; Genomic_DNA.
DR PIR; H64728; H64728.
DR RefSeq; NP_414614.1; NC_000913.3.
DR RefSeq; WP_001140652.1; NZ_STEB01000010.1.
DR AlphaFoldDB; P0A6A6; -.
DR SMR; P0A6A6; -.
DR BioGRID; 4262050; 14.
DR BioGRID; 849465; 1.
DR ComplexPortal; CPX-5159; 3-isopropylmalate dehydratase complex.
DR DIP; DIP-35834N; -.
DR IntAct; P0A6A6; 3.
DR STRING; 511145.b0072; -.
DR SWISS-2DPAGE; P0A6A6; -.
DR jPOST; P0A6A6; -.
DR PaxDb; P0A6A6; -.
DR PRIDE; P0A6A6; -.
DR EnsemblBacteria; AAC73183; AAC73183; b0072.
DR EnsemblBacteria; BAB96641; BAB96641; BAB96641.
DR GeneID; 66671638; -.
DR GeneID; 945076; -.
DR KEGG; ecj:JW0071; -.
DR KEGG; eco:b0072; -.
DR PATRIC; fig|1411691.4.peg.2209; -.
DR EchoBASE; EB1536; -.
DR eggNOG; COG0065; Bacteria.
DR HOGENOM; CLU_006714_3_4_6; -.
DR InParanoid; P0A6A6; -.
DR OMA; CNMSIEM; -.
DR PhylomeDB; P0A6A6; -.
DR BioCyc; EcoCyc:LEUC-MON; -.
DR BioCyc; MetaCyc:LEUC-MON; -.
DR UniPathway; UPA00048; UER00071.
DR PRO; PR:P0A6A6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009316; C:3-isopropylmalate dehydratase complex; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-UniRule.
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; IMP:EcoCyc.
DR CDD; cd01583; IPMI; 1.
DR Gene3D; 3.30.499.10; -; 2.
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; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR033941; IPMI_cat.
DR Pfam; PF00330; Aconitase; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; SSF53732; 1.
DR TIGRFAMs; TIGR00170; leuC; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Direct protein sequencing; Iron; Iron-sulfur; Leucine biosynthesis; Lyase;
KW Metal-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646,
FT ECO:0000269|PubMed:9600841, ECO:0000269|PubMed:9740056"
FT CHAIN 2..466
FT /note="3-isopropylmalate dehydratase large subunit"
FT /id="PRO_0000076745"
FT BINDING 347
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT BINDING 407
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT BINDING 410
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT CONFLICT 74
FT /note="A -> G (in Ref. 5; BAA21004/BAA21005)"
FT /evidence="ECO:0000305"
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
