LEU3_SULTO
ID LEU3_SULTO Reviewed; 337 AA.
AC P50455; F9VMY4; O05169;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=3-isopropylmalate dehydrogenase;
DE Short=3-IPM-DH;
DE Short=IMDH;
DE EC=1.1.1.85;
DE AltName: Full=Beta-IPM dehydrogenase;
GN Name=leuB; OrderedLocusNames=STK_04330;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=9023199; DOI=10.1128/jb.179.4.1174-1179.1997;
RA Suzuki T., Inoki Y., Yamagishi A., Iwasaki T., Wakagi T., Oshima T.;
RT "Molecular and phylogenetic characterization of isopropylmalate
RT dehydrogenase of a thermoacidophilic archaeon, Sulfolobus sp. strain 7.";
RL J. Bacteriol. 179:1174-1179(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
RN [3]
RP PROTEIN SEQUENCE OF 2-16, SUBUNIT, COFACTOR, AND CHARACTERIZATION.
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=7557336; DOI=10.1111/j.1574-6968.1995.tb07783.x;
RA Yoda E., Anraku Y., Kirino H., Wakagi T., Oshima T.;
RT "Purification and characterization of 3-isopropylmalate dehydrogenase from
RT a thermoacidophilic archaebacterium Sulfolobus sp. strain 7.";
RL FEMS Microbiol. Lett. 131:243-247(1995).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), AND SUBUNIT.
RA Hirose R., Sakurai M., Suzuki T., Moriyama H., Sato T., Yamagishi A.,
RA Oshima T., Tanaka N.;
RT "Crystal structure of IPMDH from Sulfolobus tokodaii.";
RL Submitted (OCT-2004) to the PDB data bank.
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:7557336};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:7557336};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC {ECO:0000269|PubMed:7557336};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 3/4.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:7557336, ECO:0000269|Ref.4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
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DR EMBL; D86857; BAA13178.1; -; Genomic_DNA.
DR EMBL; BA000023; BAK54281.1; -; Genomic_DNA.
DR RefSeq; WP_010978405.1; NC_003106.2.
DR PDB; 1WPW; X-ray; 2.80 A; A/B=2-337.
DR PDBsum; 1WPW; -.
DR AlphaFoldDB; P50455; -.
DR SMR; P50455; -.
DR STRING; 273063.STK_04330; -.
DR EnsemblBacteria; BAK54281; BAK54281; STK_04330.
DR GeneID; 42799970; -.
DR KEGG; sto:STK_04330; -.
DR PATRIC; fig|273063.9.peg.503; -.
DR eggNOG; arCOG01163; Archaea.
DR OMA; EYDLGAR; -.
DR OrthoDB; 33452at2157; -.
DR BRENDA; 1.1.1.85; 15396.
DR UniPathway; UPA00048; UER00072.
DR EvolutionaryTrace; P50455; -.
DR Proteomes; UP000001015; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-EC.
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-UniPathway.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR InterPro; IPR011828; LEU3_arc.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR TIGRFAMs; TIGR02088; LEU3_arch; 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;
KW Direct protein sequencing; Leucine biosynthesis; Magnesium; Manganese;
KW Metal-binding; NAD; Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7557336"
FT CHAIN 2..337
FT /note="3-isopropylmalate dehydrogenase"
FT /id="PRO_0000083812"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 258..270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 124
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT SITE 170
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1WPW"
FT HELIX 14..31
FT /evidence="ECO:0007829|PDB:1WPW"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:1WPW"
FT HELIX 45..50
FT /evidence="ECO:0007829|PDB:1WPW"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:1WPW"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:1WPW"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:1WPW"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:1WPW"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:1WPW"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:1WPW"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:1WPW"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:1WPW"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:1WPW"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:1WPW"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:1WPW"
FT STRAND 135..143
FT /evidence="ECO:0007829|PDB:1WPW"
FT HELIX 144..159
FT /evidence="ECO:0007829|PDB:1WPW"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:1WPW"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:1WPW"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:1WPW"
FT HELIX 177..189
FT /evidence="ECO:0007829|PDB:1WPW"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:1WPW"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:1WPW"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:1WPW"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:1WPW"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:1WPW"
FT HELIX 221..235
FT /evidence="ECO:0007829|PDB:1WPW"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:1WPW"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:1WPW"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:1WPW"
FT TURN 261..265
FT /evidence="ECO:0007829|PDB:1WPW"
FT HELIX 272..287
FT /evidence="ECO:0007829|PDB:1WPW"
FT HELIX 293..311
FT /evidence="ECO:0007829|PDB:1WPW"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:1WPW"
FT HELIX 325..334
FT /evidence="ECO:0007829|PDB:1WPW"
SQ SEQUENCE 337 AA; 36964 MW; 1B44CB9A0CD70313 CRC64;
MGFTVALIQG DGIGPEIVSK SKRILAKINE LYSLPIEYIE VEAGDRALAR YGEALPKDSL
KIIDKADIIL KGPVGESAAD VVVKLRQIYD MYANIRPAKS IPGIDTKYGN VDILIVRENT
EDLYKGFEHI VSDGVAVGMK IITRFASERI AKVGLNFALR RRKKVTCVHK ANVMRITDGL
FAEACRSVLK GKVEYSEMYV DAAAANLVRN PQMFDVIVTE NVYGDILSDE ASQIAGSLGI
APSANIGDKK ALFEPVHGAA FDIAGKNIGN PTAFLLSVSM MYERMYELSN DDRYIKASRA
LENAIYLVYK ERKALTPDVG GNATTDDLIN EIYNKLG
