LEU3_AGRFC
ID LEU3_AGRFC Reviewed; 370 AA.
AC P24404;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=3-isopropylmalate dehydrogenase;
DE EC=1.1.1.85;
DE AltName: Full=3-IPM-DH;
DE AltName: Full=Beta-IPM dehydrogenase;
DE Short=IMDH;
GN Name=leuB; OrderedLocusNames=Atu2791; ORFNames=AGR_C_5067;
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Strizhov N.I., Kryukov V.M., Bur'Yanov Y.I., Beav A.A.;
RT "Beta-isopropyl malate dehydrogenase gene of Agrobacterium tumefaciens C58:
RT coding and primary structure.";
RL Dokl. Akad. Nauk SSSR 288:481-486(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
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 (By similarity). {ECO:0000250}.
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 3/4.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. LeuB type 1 subfamily. {ECO:0000305}.
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DR EMBL; M38670; AAA22089.1; -; Genomic_DNA.
DR EMBL; AE007869; AAK88504.1; -; Genomic_DNA.
DR PIR; AF2919; AF2919.
DR PIR; G97693; G97693.
DR RefSeq; NP_355719.1; NC_003062.2.
DR RefSeq; WP_010972566.1; NC_003062.2.
DR AlphaFoldDB; P24404; -.
DR SMR; P24404; -.
DR STRING; 176299.Atu2791; -.
DR EnsemblBacteria; AAK88504; AAK88504; Atu2791.
DR KEGG; atu:Atu2791; -.
DR PATRIC; fig|176299.10.peg.2801; -.
DR eggNOG; COG0473; Bacteria.
DR HOGENOM; CLU_031953_0_3_5; -.
DR OMA; EYDLGAR; -.
DR PhylomeDB; P24404; -.
DR BioCyc; AGRO:ATU2791-MON; -.
DR BRENDA; 1.1.1.85; 200.
DR UniPathway; UPA00048; UER00072.
DR Proteomes; UP000000813; Chromosome circular.
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..370
FT /note="3-isopropylmalate dehydrogenase"
FT /id="PRO_0000083627"
FT BINDING 77..90
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 290..302
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 142
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT SITE 193
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 6
FT /note="L -> V (in Ref. 1; AAA22089)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 370 AA; 39659 MW; BB4138D257849E0B CRC64;
MTVRSLFLLP GDGIGPEAMT EVRKLIEYMN SAHNAGFTVS EGLVGGSAYD AHGVAISDAD
MEKALAADAI LFGAVGGPKW DGVPYEHRPE AGLLRLRKDL ELFANLRPAI CYPALAAASS
LKPELVEGLD ILIVRELTGG VYFGEPKQII DLGNGQKRGI DTQIYDTFEI ERIASVAFEL
ARSRDNRVCS MEKRNVMKSG VLWNQVVTET HAAKYKDVQL EHMLADAGGM QLVRKPKQFD
VIVTDNLFGD MLSDVAAMLT GSLGMLPSAS LGAPDAKTGK RKAMYEPVHG SAPDIAGKSI
ANPIAMIASF AMCLRYSFNM VDEATKLEAA IANVLDKGIR TADIMADGCR QVGTSDMGDA
VLAEFKALSA
