(data stored in ACNUC7421 zone)

SWISSPROT: LEU3_THEFY

ID   LEU3_THEFY              Reviewed;         354 AA.
AC   Q47SB4;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 98.
DE   RecName: Full=3-isopropylmalate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01035};
DE            EC=1.1.1.85 {ECO:0000255|HAMAP-Rule:MF_01035};
DE   AltName: Full=3-IPM-DH {ECO:0000255|HAMAP-Rule:MF_01035};
DE   AltName: Full=Beta-IPM dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01035};
DE            Short=IMDH {ECO:0000255|HAMAP-Rule:MF_01035};
GN   Name=leuB {ECO:0000255|HAMAP-Rule:MF_01035};
GN   OrderedLocusNames=Tfu_0615;
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX;
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-
CC       methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-
CC       oxopentanoate. The product decarboxylates to 4-methyl-2
CC       oxopentanoate. {ECO:0000255|HAMAP-Rule:MF_01035}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-
CC         oxopentanoate + CO2 + NADH; Xref=Rhea:RHEA:32271,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:17865, ChEBI:CHEBI:35121,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.85;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01035};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01035};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01035};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01035};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC       leucine from 3-methyl-2-oxobutanoate: step 3/4.
CC       {ECO:0000255|HAMAP-Rule:MF_01035}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01035}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01035}.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. LeuB type 2 subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01035}.
DR   EMBL; CP000088; AAZ54653.1; -; Genomic_DNA.
DR   RefSeq; WP_011291062.1; NC_007333.1.
DR   SMR; Q47SB4; -.
DR   STRING; 269800.Tfu_0615; -.
DR   EnsemblBacteria; AAZ54653; AAZ54653; Tfu_0615.
DR   KEGG; tfu:Tfu_0615; -.
DR   eggNOG; ENOG4105C0C; Bacteria.
DR   eggNOG; COG0473; LUCA.
DR   HOGENOM; HOG000021111; -.
DR   KO; K00052; -.
DR   OMA; EYDLGAR; -.
DR   OrthoDB; 1551125at2; -.
DR   BioCyc; TFUS269800:G1G4Q-626-MONOMER; -.
DR   UniPathway; UPA00048; UER00072.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01035; LeuB_type2; 1.
DR   InterPro; IPR023698; 3-isopropylmalate_DH_LeuB.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   Pfam; PF00180; Iso_dh; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47SB4.
DR   SWISS-2DPAGE; Q47SB4.
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Complete proteome; Cytoplasm; Leucine biosynthesis; Magnesium;
KW   Manganese; Metal-binding; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN         1    354       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000083807.
FT   NP_BIND     283    295       NAD. {ECO:0000255|HAMAP-Rule:MF_01035}.
FT   METAL       223    223       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01035}.
FT   METAL       247    247       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01035}.
FT   METAL       251    251       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01035}.
FT   BINDING      96     96       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01035}.
FT   BINDING     106    106       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01035}.
FT   BINDING     132    132       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01035}.
FT   BINDING     223    223       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01035}.
FT   SITE        139    139       Important for catalysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_01035}.
FT   SITE        190    190       Important for catalysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_01035}.
SQ   SEQUENCE   354 AA;  37836 MW;  1AAD0E89978BB5FA CRC64;
     MSARTVKLAV IPGDGIGPEV VAEGLKVLSA VAPRHGLTLD TTEYELGAQR WHATGEVLPD
     AVEEELRQHD AILLGAVGDP TVPSGVLERG LLLRLRFNFS HYVNLRPVRL YPGVTTPLAG
     VAPEDIDMLV VREGTEGPYA GMGGVLRKGT PHEIATQDSV NTRLGVERVV RYAFAKAAER
     PCHKLTLVHK DNVLTYAGEL WQRVVREVGA EYPQVEVDYL HVDAATMFFV TQPRRFDVVV
     TDNLFGDIIT DLGAAVAGGI GLAASGNINP EGDFPSMFEP VHGSAPDIAG QGKADPTATI
     LSVSLMLEHL GYADAAAQID QAVAEDLQER AKNGGVRSTT QIGDDIAQRV AEQG
//

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