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LEU3_VIBVY
ID   LEU3_VIBVY              Reviewed;         363 AA.
AC   Q7MP78;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 122.
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}; OrderedLocusNames=VV0486;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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_01033}.
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_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-leucine
CC       from 3-methyl-2-oxobutanoate: step 3/4. {ECO:0000255|HAMAP-
CC       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}.
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DR   EMBL; BA000037; BAC93250.1; -; Genomic_DNA.
DR   RefSeq; WP_011149404.1; NC_005139.1.
DR   AlphaFoldDB; Q7MP78; -.
DR   SMR; Q7MP78; -.
DR   STRING; 672.VV93_v1c04540; -.
DR   EnsemblBacteria; BAC93250; BAC93250; BAC93250.
DR   KEGG; vvy:VV0486; -.
DR   PATRIC; fig|196600.6.peg.512; -.
DR   eggNOG; COG0473; Bacteria.
DR   HOGENOM; CLU_031953_0_3_6; -.
DR   OMA; EYDLGAR; -.
DR   OrthoDB; 1551125at2; -.
DR   UniPathway; UPA00048; UER00072.
DR   Proteomes; UP000002675; Chromosome I.
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_01033; LeuB_type1; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   InterPro; IPR004429; Isopropylmalate_DH.
DR   PANTHER; PTHR42979; PTHR42979; 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; Cytoplasm;
KW   Leucine biosynthesis; Magnesium; Manganese; Metal-binding; NAD;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..363
FT                   /note="3-isopropylmalate dehydrogenase"
FT                   /id="PRO_0000083782"
FT   BINDING         79..92
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT   BINDING         110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT   BINDING         228
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT   BINDING         228
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT   BINDING         252
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT   BINDING         256
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT   BINDING         286..298
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT   SITE            146
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT   SITE            196
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
SQ   SEQUENCE   363 AA;  39391 MW;  F9235D11D6DCD4FD CRC64;
     MTDKTYKIAV LPGDGIGPEV MAQAHKVLDA IEKKHAIHFE REEHDVGGIA IDNHGCPLPQ
     STVTACEESD AVLFGSVGGP KWEHLPPNDQ PERGALLPLR KHFQLFCNLR PAQIHSGLEA
     FSPLRADISG RGFDIVVVRE LTGGIYFGQP KGREGEGANE KAYDTEIYHR FEIERIAKIA
     FESARLRRKK VCSIDKANVL QSSILWREVV EEIAKDYPDV ELSHMYIDNA TMQLIKDPAQ
     FDVMLCSNIF GDIISDECAM ITGSMGMLPS ASLNESKFGL YEPAGGSAPD IAGKNIANPV
     AQILSAALML RYSLGEEAAA QDIENAVSQA LAAGELTADL AGDKPALSTA EMGDKIAQYI
     LNS
 
 
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