LEU3_CAMJE
ID LEU3_CAMJE Reviewed; 358 AA.
AC Q9PLW0; Q0P7R3;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
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=Cj1718c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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 -!- 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; AL111168; CAL35812.1; -; Genomic_DNA.
DR PIR; B81270; B81270.
DR RefSeq; WP_002858793.1; NC_002163.1.
DR RefSeq; YP_002345084.1; NC_002163.1.
DR PDB; 3UDO; X-ray; 2.30 A; A=1-358.
DR PDB; 3UDU; X-ray; 1.85 A; A/B/C/D/E/F/G/H=1-358.
DR PDBsum; 3UDO; -.
DR PDBsum; 3UDU; -.
DR AlphaFoldDB; Q9PLW0; -.
DR SMR; Q9PLW0; -.
DR IntAct; Q9PLW0; 6.
DR STRING; 192222.Cj1718c; -.
DR PaxDb; Q9PLW0; -.
DR PRIDE; Q9PLW0; -.
DR EnsemblBacteria; CAL35812; CAL35812; Cj1718c.
DR GeneID; 905995; -.
DR KEGG; cje:Cj1718c; -.
DR PATRIC; fig|192222.6.peg.1692; -.
DR eggNOG; COG0473; Bacteria.
DR HOGENOM; CLU_031953_0_3_7; -.
DR OMA; EYDLGAR; -.
DR UniPathway; UPA00048; UER00072.
DR Proteomes; UP000000799; 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_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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; Cytoplasm; Leucine biosynthesis;
KW Magnesium; Manganese; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..358
FT /note="3-isopropylmalate dehydrogenase"
FT /id="PRO_0000083675"
FT BINDING 77..90
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 221
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 279..291
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT SITE 144
FT /note="Important for catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT SITE 189
FT /note="Important for catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:3UDU"
FT HELIX 15..33
FT /evidence="ECO:0007829|PDB:3UDU"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:3UDU"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:3UDU"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:3UDU"
FT HELIX 58..65
FT /evidence="ECO:0007829|PDB:3UDU"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:3UDU"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:3UDU"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:3UDU"
FT HELIX 89..101
FT /evidence="ECO:0007829|PDB:3UDU"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:3UDU"
FT HELIX 114..119
FT /evidence="ECO:0007829|PDB:3UDU"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:3UDU"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:3UDU"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:3UDU"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:3UDU"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:3UDU"
FT STRAND 152..162
FT /evidence="ECO:0007829|PDB:3UDU"
FT HELIX 163..179
FT /evidence="ECO:0007829|PDB:3UDU"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:3UDU"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:3UDU"
FT HELIX 194..206
FT /evidence="ECO:0007829|PDB:3UDU"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:3UDU"
FT STRAND 213..219
FT /evidence="ECO:0007829|PDB:3UDU"
FT HELIX 220..229
FT /evidence="ECO:0007829|PDB:3UDU"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:3UDU"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:3UDU"
FT HELIX 241..255
FT /evidence="ECO:0007829|PDB:3UDU"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:3UDU"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:3UDU"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:3UDO"
FT STRAND 272..278
FT /evidence="ECO:0007829|PDB:3UDU"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:3UDU"
FT HELIX 293..305
FT /evidence="ECO:0007829|PDB:3UDU"
FT HELIX 310..325
FT /evidence="ECO:0007829|PDB:3UDU"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:3UDU"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:3UDU"
FT HELIX 341..354
FT /evidence="ECO:0007829|PDB:3UDU"
SQ SEQUENCE 358 AA; 39368 MW; 26B811645E7FFA83 CRC64;
MKTYKVAVLA GDGIGPLVMK EALKILTFIA QKYNFSFEFN EAKIGGASID AYGVALSDET
LKLCEQSDAI LFGSVGGPKW DNLPIDQRPE RASLLPLRKH FNLFANLRPC KIYESLTHAS
PLKNEIIQKG VDILCVRELT GGIYFGKQDL GKESAYDTEI YTKKEIERIA RIAFESARIR
KKKVHLIDKA NVLASSILWR EVVANVAKDY QDINLEYMYV DNAAMQIVKN PSIFDVMLCS
NLFGDILSDE LAAINGSLGL LSSASLNDKG FGLYEPAGGS APDIAHLNIA NPIAQILSAA
LMLKYSFKEE QAAQDIENAI SLALAQGKMT KDLNAKSYLN TDEMGDCILE ILKENDNG
