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Database: UniProt/SWISS-PROT
Entry: LEUD_NEIG1
LinkDB: LEUD_NEIG1
Original site: LEUD_NEIG1 
ID   LEUD_NEIG1              Reviewed;         213 AA.
AC   Q5F8T3;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   19-FEB-2014, entry version 61.
DE   RecName: Full=3-isopropylmalate dehydratase small subunit;
DE            EC=4.2.1.33;
DE   AltName: Full=Alpha-IPM isomerase;
DE            Short=IPMI;
DE   AltName: Full=Isopropylmalate isomerase;
GN   Name=leuD; OrderedLocusNames=NGO0677;
OS   Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=242231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700825 / FA 1090;
RA   Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA   Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA   Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA   Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT   "The complete genome sequence of Neisseria gonorrhoeae.";
RL   Submitted (MAR-2003) 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   -!- 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 LeuD family. LeuD type 1 subfamily.
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DR   EMBL; AE004969; AAW89404.1; -; Genomic_DNA.
DR   RefSeq; YP_207816.1; NC_002946.2.
DR   ProteinModelPortal; Q5F8T3; -.
DR   STRING; 242231.NGO0677; -.
DR   PRIDE; Q5F8T3; -.
DR   EnsemblBacteria; AAW89404; AAW89404; NGO0677.
DR   GeneID; 3282001; -.
DR   KEGG; ngo:NGO0677; -.
DR   PATRIC; 20334452; VBINeiGon24812_0798.
DR   eggNOG; COG0066; -.
DR   HOGENOM; HOG000222939; -.
DR   KO; K01704; -.
DR   OMA; AFTTHTG; -.
DR   OrthoDB; EOG661HCP; -.
DR   ProtClustDB; PRK01641; -.
DR   BioCyc; NGON242231:GI2G-644-MONOMER; -.
DR   UniPathway; UPA00048; UER00071.
DR   GO; GO:0009316; C:3-isopropylmalate dehydratase complex; IEA:InterPro.
DR   GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.19.10; -; 1.
DR   HAMAP; MF_01031; LeuD_type1; 1.
DR   InterPro; IPR004431; 3-IsopropMal_deHydase_ssu.
DR   InterPro; IPR015937; Acoase/IPM_deHydtase.
DR   InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   PANTHER; PTHR11670; PTHR11670; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   SUPFAM; SSF52016; SSF52016; 1.
DR   TIGRFAMs; TIGR00171; leuD; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Complete proteome; Leucine biosynthesis; Lyase; Reference proteome.
FT   CHAIN         1    213       3-isopropylmalate dehydratase small
FT                                subunit.
FT                                /FTId=PRO_0000141842.
SQ   SEQUENCE   213 AA;  24208 MW;  0835E832C3FE3C82 CRC64;
     MKAFTKITAI VAPLDRSNVD TDAIIPKQFL KSIKRSGFGP NAFDEWRYLD HGEPGMDNGK
     RPLNPDFSLN QPRYQGAQIL LTRKNFGCGS SREHAPWALD DYGFRAIIAP SFADIFFNNC
     YKNGLLPIVL TEEQVDRLFK EVEANEGYRL SIDLAEQTLT TPGGETFTFD ITEHRKHCLL
     NGLDEIGLTL QHADKIKAFE EKRRQSQPWL FNG
//
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