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Database: UniProt
Entry: Q47SB4
LinkDB: Q47SB4
Original site: Q47SB4 
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   27-MAR-2024, entry version 123.
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}; OrderedLocusNames=Tfu_0615;
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; 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., DiBartolo G.,
RA   Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA   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 oxopentanoate.
CC       {ECO:0000255|HAMAP-Rule:MF_01035}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate
CC         + CO2 + NADH; Xref=Rhea:RHEA:32271, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17865, ChEBI:CHEBI:35121, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.1.1.85; Evidence={ECO:0000255|HAMAP-
CC         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-leucine
CC       from 3-methyl-2-oxobutanoate: step 3/4. {ECO:0000255|HAMAP-
CC       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}.
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DR   EMBL; CP000088; AAZ54653.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q47SB4; -.
DR   SMR; Q47SB4; -.
DR   STRING; 269800.Tfu_0615; -.
DR   KEGG; tfu:Tfu_0615; -.
DR   eggNOG; COG0473; Bacteria.
DR   HOGENOM; CLU_031953_0_1_11; -.
DR   OrthoDB; 5289857at2; -.
DR   UniPathway; UPA00048; UER00072.
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   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   HAMAP; MF_01035; LeuB_type2; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   InterPro; IPR023698; LeuB_actb.
DR   PANTHER; PTHR43275; D-MALATE DEHYDROGENASE [DECARBOXYLATING]; 1.
DR   PANTHER; PTHR43275:SF1; D-MALATE DEHYDROGENASE [DECARBOXYLATING]; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Cytoplasm;
KW   Leucine biosynthesis; Magnesium; Manganese; Metal-binding; NAD;
KW   Oxidoreductase.
FT   CHAIN           1..354
FT                   /note="3-isopropylmalate dehydrogenase"
FT                   /id="PRO_0000083807"
FT   BINDING         96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT   BINDING         132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT   BINDING         223
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT   BINDING         223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT   BINDING         247
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT   BINDING         251
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT   BINDING         283..295
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT   SITE            139
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT   SITE            190
FT                   /note="Important for catalysis"
FT                   /evidence="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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