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Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7

DescriptionRecName: Full=3-isopropylmalate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01033}; EC=1.1.1.85 {ECO:0000255|HAMAP-Rule:MF_01033}; AltName: Full=3-IPM-DH {ECO:0000255|HAMAP-Rule:MF_01033}; AltName: Full=Beta-IPM dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01033}; Short=IMDH {ECO:0000255|HAMAP-Rule:MF_01033};
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MyHits synonymsLEU3_RHORT , Q2RV53 , EB6B4847C8DF8B6B
match map segment
ipfam:Iso_dh ihamap:LeuB_type1 ismart:Iso_dh ipat:IDH_IMDH  
Legends: 1, Magnesium or manganese. {ECO:0000255|HAMAP-Rule:MF_01033}; 2, BINDING Substrate. {ECO:0000255|HAMAP- Rule:MF_01033}; 3, SITE Important for catalysis. {ECO:0000255|HAMAP-Rule:MF_01033}; 4, NP_BIND NAD. {ECO:0000255|HAMAP-Rule:MF_01033}; 5, ipat:IDH_IMDH [T].
ID   LEU3_RHORT              Reviewed;         370 AA.
AC   Q2RV53;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   02-NOV-2016, entry version 79.
DE   RecName: Full=3-isopropylmalate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01033};
DE            EC=1.1.1.85 {ECO:0000255|HAMAP-Rule:MF_01033};
DE   AltName: Full=3-IPM-DH {ECO:0000255|HAMAP-Rule:MF_01033};
DE   AltName: Full=Beta-IPM dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01033};
DE            Short=IMDH {ECO:0000255|HAMAP-Rule:MF_01033};
GN   Name=leuB {ECO:0000255|HAMAP-Rule:MF_01033};
GN   OrderedLocusNames=Rru_A1191;
OS   Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG
OS   4362 / NCIB 8255 / S1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G.,
RA   Reslewic S., Zhou S., Schwartz D.C.;
RT   "Complete sequence of the chromosome of Rhodospirillum rubrum ATCC
RT   11170.";
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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_01033}.
CC   -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-
CC       2-oxopentanoate + CO(2) + NADH. {ECO:0000255|HAMAP-Rule:MF_01033}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01033};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01033};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01033};
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_01033}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01033}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01033}.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. LeuB type 1 subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01033}.
DR   EMBL; CP000230; ABC21992.1; -; Genomic_DNA.
DR   RefSeq; WP_011388946.1; NC_007643.1.
DR   RefSeq; YP_426279.1; NC_007643.1.
DR   ProteinModelPortal; Q2RV53; -.
DR   STRING; 269796.Rru_A1191; -.
DR   PRIDE; Q2RV53; -.
DR   EnsemblBacteria; ABC21992; ABC21992; Rru_A1191.
DR   GeneID; 3834701; -.
DR   KEGG; rru:Rru_A1191; -.
DR   PATRIC; 23325994; VBIRhoRub82919_1255.
DR   eggNOG; ENOG4105C0C; Bacteria.
DR   eggNOG; COG0473; LUCA.
DR   HOGENOM; HOG000021112; -.
DR   KO; K00052; -.
DR   OMA; RRPKQFD; -.
DR   OrthoDB; POG091H01YH; -.
DR   UniPathway; UPA00048; UER00072.
DR   Proteomes; UP000001929; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.718.10; -; 1.
DR   HAMAP; MF_01033; LeuB_type1; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR001804; Isocitrate/isopropylmalate_DH.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   InterPro; IPR004429; Isopropylmalate_DH.
DR   PANTHER; PTHR11835; PTHR11835; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   TIGRFAMs; TIGR00169; leuB; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   3: Inferred from homology;
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    370       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000250135.
FT   NP_BIND     290    302       NAD. {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   METAL       227    227       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   METAL       251    251       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   METAL       255    255       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   BINDING      99     99       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01033}.
FT   BINDING     109    109       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01033}.
FT   BINDING     137    137       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01033}.
FT   BINDING     227    227       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01033}.
FT   SITE        144    144       Important for catalysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   SITE        195    195       Important for catalysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_01033}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT         6    360       ipfam:Iso_dh [T]
FT   MYHIT         5    365       ihamap:LeuB_type1 [T]
FT   MYHIT         6    361       ismart:Iso_dh [T]
FT   MYHIT       247    266       ipat:IDH_IMDH [T]
SQ   SEQUENCE   370 AA;  39536 MW;  EB6B4847C8DF8B6B CRC64;
     MPVSKKILFL AGDGIGPEVM AQVRRVMDWL NQTGRTAFEV EDALVGGAAY DAQGTPLHDD
     TVALALAADA VLLGAVGGPK WDASLPFELK PERGLLRLRK DLELFANLRP AMVFDALAEA
     STLKTELVSG LDVMIVRELT GGVYFGQPRG ISALPNGERR GVNTQVYDTH EIVRVAKVAF
     DLAGKRGKRL CSVEKANVME SGLLWREEVT KLGADYPEIA LSHMYADNCA MQLVRQPKQF
     DVIVTDNLFG DILSDCAAML TGSLGMLPSA SLGAADAAGN RRAMYEPVHG SAPDIAGQDK
     ANPLATILSF SMMLRYSFDL AEEADLVDNA VRGVLAKGLR TGDIFQPGKT LVGTTGMGDA
     LLAEMAQLAN
//