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 01-MAY-2013, entry version 56.
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; YQDNSKR; -.
DR ProtClustDB; PRK01641; -.
DR BioCyc; NGON242231:GI2G-632-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:HAMAP.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:HAMAP.
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 PANTHER; PTHR11670:SF2; PTHR11670:SF2; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR SUPFAM; SSF52016; Aconitase/3IPM_dehydase_swvl; 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
//
