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LEU3_MYCMM
ID   LEU3_MYCMM              Reviewed;         339 AA.
AC   B2HIH1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=MMAR_1716;
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=216594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M;
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
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; CP000854; ACC40165.1; -; Genomic_DNA.
DR   RefSeq; WP_012393531.1; NC_010612.1.
DR   AlphaFoldDB; B2HIH1; -.
DR   SMR; B2HIH1; -.
DR   STRING; 216594.MMAR_1716; -.
DR   EnsemblBacteria; ACC40165; ACC40165; MMAR_1716.
DR   GeneID; 64260411; -.
DR   KEGG; mmi:MMAR_1716; -.
DR   eggNOG; COG0473; Bacteria.
DR   HOGENOM; CLU_031953_0_1_11; -.
DR   OMA; EYDLGAR; -.
DR   OrthoDB; 1551125at2; -.
DR   UniPathway; UPA00048; UER00072.
DR   Proteomes; UP000001190; 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; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   InterPro; IPR023698; LeuB_actb.
DR   Pfam; PF00180; Iso_dh; 1.
DR   SMART; SM01329; Iso_dh; 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; Reference proteome.
FT   CHAIN           1..339
FT                   /note="3-isopropylmalate dehydrogenase"
FT                   /id="PRO_1000135857"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT   BINDING         124
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT   BINDING         214
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT   BINDING         214
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT   BINDING         238
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT   BINDING         242
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT   BINDING         274..286
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT   SITE            131
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT   SITE            181
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
SQ   SEQUENCE   339 AA;  36046 MW;  A7CC1DA45644CC33 CRC64;
     MKLAIVAGDG IGPEVVAQAV KVLDVVQPGV EKTNYDLGAR RFHATGEILP DSVIAELREH
     DAILLGAIGD PSVPSGVLER GLLLRLRFEL DHHINLRPGR LYPGVKSPLA LEPGNPEIDF
     VVVREGTEGP YTGNGGAIRV GTANEVATEV SVNTAFGVRR VVRDAFERAM RRRKHLTLVH
     KNNVLTFAGS LWWRTVQEIG EEYPDVELAY QHVDAATIHM VTDPGRFDVI VTDNLFGDII
     TDLAAAVCGG IGLAASGNID ATRTNPSMFE PVHGSAPDIA GQGIADPTAA IMSVSLLLAH
     LGLDDAASRV DRAVEGYLAT RGNERLATAA VGERIAAAL
 
 
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