(data stored in ACNUC7421 zone)

SWISSPROT: LEUC_SHESH

ID   LEUC_SHESH              Reviewed;         466 AA.
AC   A8FQ85;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 70.
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=Ssed_0395;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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: (2R,3S)-3-isopropylmalate = (2S)-2-
CC       isopropylmalate. {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; CP000821; ABV35008.1; -; Genomic_DNA.
DR   RefSeq; WP_012140745.1; NC_009831.1.
DR   ProteinModelPortal; A8FQ85; -.
DR   SMR; A8FQ85; -.
DR   STRING; 425104.Ssed_0395; -.
DR   PRIDE; A8FQ85; -.
DR   EnsemblBacteria; ABV35008; ABV35008; Ssed_0395.
DR   KEGG; sse:Ssed_0395; -.
DR   eggNOG; ENOG4105CQI; Bacteria.
DR   eggNOG; COG0065; LUCA.
DR   HOGENOM; HOG000226972; -.
DR   KO; K01703; -.
DR   OMA; CNMSIEM; -.
DR   OrthoDB; POG091H02GD; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-EC.
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-UniPathway.
DR   CDD; cd01583; IPMI; 1.
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; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR   InterPro; IPR015932; Aconitase/IPMdHydase_lsu_aba_2.
DR   InterPro; IPR018136; Aconitase_4Fe-4S_BS.
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; A8FQ85.
DR   SWISS-2DPAGE; A8FQ85.
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_1000084228.
FT   METAL       347    347       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01026}.
FT   METAL       407    407       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01026}.
FT   METAL       410    410       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01026}.
SQ   SEQUENCE   466 AA;  49637 MW;  9922047F3DA7A3AF CRC64;
     MAKTLYEKVW DSHVVVENEG QAPLIYVDRH LVHEVTSPQA FSGLKVAGRK LRAPEKTFAT
     MDHNTSTKSA SLDALSPMAR IQVETLQDNC KEFGVRLYDI HHKNQGIVHV MGPELGITLP
     GTVIVCGDSH TATHGAFGAL AFGIGTSEVE HVMATQTLRQ NKAKTMKIEV RGHVAAGITA
     KDIVLAIIGK IGMDGGTGYV VEFCGEAIEA LSMEGRMTVC NMAIEMGAKA GMVAPDGITA
     EYLKGREFAP KGESWEQAIA AWAELKTDED AIFDASVVLE ASDIAPQLTW GTNPGQVVAI
     DGLVPNPEDE SNATVKASIE KALEYVALSA GTCMTDVSIN KVFIGSCTNS RIEDLRDAAL
     HAKGRKVAAG VTAIVVPGSG LVKEQAEAEG LDKIFLEAGF EWRLPGCSMC LAMNDDRLEA
     GDRCASTSNR NFEGRQGRGS RTHLVSPAMA AAAAVAGHFV DIRKAY
//

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