(data stored in ACNUC7421 zone)

SWISSPROT: LEUC_RUEPO

ID   LEUC_RUEPO              Reviewed;         468 AA.
AC   Q5LX06;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 91.
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=SPO0216;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C.,
RA   Brinkac L.M., Lewis M., Johri S., Weaver B., Pai G., Eisen J.A.,
RA   Rahe E., Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., DeBoy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
CC   -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate
CC       and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
CC       {ECO:0000255|HAMAP-Rule:MF_01026}.
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-
CC       leucine from 3-methyl-2-oxobutanoate: step 2/4.
CC       {ECO:0000255|HAMAP-Rule:MF_01026}.
CC   -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000255|HAMAP-
CC       Rule:MF_01026}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC
CC       type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01026}.
DR   EMBL; CP000031; AAV93541.1; -; Genomic_DNA.
DR   RefSeq; WP_011045984.1; NC_003911.12.
DR   STRING; 246200.SPO0216; -.
DR   PRIDE; Q5LX06; -.
DR   DNASU; 3195137; -.
DR   EnsemblBacteria; AAV93541; AAV93541; SPO0216.
DR   KEGG; sil:SPO0216; -.
DR   eggNOG; ENOG4105CQI; Bacteria.
DR   eggNOG; COG0065; LUCA.
DR   HOGENOM; HOG000226972; -.
DR   KO; K01703; -.
DR   OMA; FDHQVPA; -.
DR   OrthoDB; 749418at2; -.
DR   BioCyc; RPOM246200:G1G48-220-MONOMER; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000001023; Chromosome.
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; IEA:UniProtKB-UniRule.
DR   CDD; cd01583; IPMI; 1.
DR   Gene3D; 3.30.499.10; -; 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; 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   3: Inferred from homology;
DR   PRODOM; Q5LX06.
DR   SWISS-2DPAGE; Q5LX06.
KW   4Fe-4S; Amino-acid biosynthesis;
KW   Branched-chain amino acid biosynthesis; Complete proteome; Iron;
KW   Iron-sulfur; Leucine biosynthesis; Lyase; Metal-binding;
KW   Reference proteome.
FT   CHAIN         1    468       3-isopropylmalate dehydratase large
FT                                subunit.
FT                                /FTId=PRO_0000076810.
FT   METAL       349    349       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01026}.
FT   METAL       409    409       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01026}.
FT   METAL       412    412       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01026}.
SQ   SEQUENCE   468 AA;  50362 MW;  0E275677F5C36DE1 CRC64;
     MSPKTLYDKI WDAHLAHEAE DGTCLLYIDR HLVHEVTSPQ AFEGLRMAGR KVRAPEKTIA
     VPDHNVPTTE GREDPAQMTE ESRIQVQALD KNAREFGVHY YPVDDIRQGI VHIVGPEQGW
     TLPGMTVVCG DSHTATHGAF GALAHGIGTS EVEHVLATQT LIQKKSKNMK VEITGKLNPG
     VTAKDITLAV IGATGTAGGT GYVIEYCGEA IRDLSMEGRM TVCNMAIEGG ARAGLIAPDQ
     TTFDYVKGRP HAPKGAQWEA ALAWWKTLYS DDGAHFDKIV TLKGEEIEPV VTWGTSPEDV
     LPITGVVPSP EDFTGGKVEA ARRSIEYMGL TPGQKLTDIE IDTVFIGSCT NGRIEDLRAV
     AEVVKGKKIK SGLRAMVVPG SGLVRAQAEE EGIADILKDA GFEWRLAGCS MCLAMNPDQL
     APGERCAATS NRNFEGRQGY KGRTHLVSPA MAAAAALTGK LTDVRELI
//

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