LEU3_HAEIN
ID LEU3_HAEIN Reviewed; 358 AA.
AC P43860;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 140.
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=HI_0987;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. LeuB type 1 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L42023; AAC22648.1; -; Genomic_DNA.
DR PIR; F64106; F64106.
DR RefSeq; NP_439150.1; NC_000907.1.
DR RefSeq; WP_005693328.1; NC_000907.1.
DR PDB; 6XXY; X-ray; 2.09 A; A/B=1-358.
DR PDBsum; 6XXY; -.
DR AlphaFoldDB; P43860; -.
DR SMR; P43860; -.
DR STRING; 71421.HI_0987; -.
DR EnsemblBacteria; AAC22648; AAC22648; HI_0987.
DR KEGG; hin:HI_0987; -.
DR PATRIC; fig|71421.8.peg.1030; -.
DR eggNOG; COG0473; Bacteria.
DR HOGENOM; CLU_031953_0_3_6; -.
DR OMA; EYDLGAR; -.
DR PhylomeDB; P43860; -.
DR BioCyc; HINF71421:G1GJ1-1029-MON; -.
DR UniPathway; UPA00048; UER00072.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IBA:GO_Central.
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; IBA:GO_Central.
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_0000083698"
FT BINDING 77..90
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 137
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 284..296
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 144
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT SITE 194
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:6XXY"
FT HELIX 15..33
FT /evidence="ECO:0007829|PDB:6XXY"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:6XXY"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:6XXY"
FT HELIX 58..65
FT /evidence="ECO:0007829|PDB:6XXY"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:6XXY"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:6XXY"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:6XXY"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:6XXY"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:6XXY"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:6XXY"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:6XXY"
FT HELIX 124..128
FT /evidence="ECO:0007829|PDB:6XXY"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:6XXY"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:6XXY"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:6XXY"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:6XXY"
FT STRAND 159..167
FT /evidence="ECO:0007829|PDB:6XXY"
FT HELIX 168..183
FT /evidence="ECO:0007829|PDB:6XXY"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:6XXY"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:6XXY"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:6XXY"
FT HELIX 199..212
FT /evidence="ECO:0007829|PDB:6XXY"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:6XXY"
FT HELIX 225..234
FT /evidence="ECO:0007829|PDB:6XXY"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:6XXY"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:6XXY"
FT HELIX 246..259
FT /evidence="ECO:0007829|PDB:6XXY"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:6XXY"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:6XXY"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:6XXY"
FT TURN 287..291
FT /evidence="ECO:0007829|PDB:6XXY"
FT HELIX 298..312
FT /evidence="ECO:0007829|PDB:6XXY"
FT HELIX 315..330
FT /evidence="ECO:0007829|PDB:6XXY"
FT HELIX 347..356
FT /evidence="ECO:0007829|PDB:6XXY"
SQ SEQUENCE 358 AA; 38808 MW; 35727EEC16A32CB6 CRC64;
MQSYNIAVLA GDGIGPEVMA EAIKVLNRVQ EKFGFKLNFN EFFVGGAAIE HCGYPLPAET
LKGCDQADAI LFGSVGGPKW TNLPPDQQPE RGALLPLRKH FKLFCNLRPA TLYKGLEKFC
PLRADIAAKG FDMVVVRELT GGIYFGQPKG REGDGVQTKA FDTEVYYKYE IERIARAAFE
AAMKRNKKVT SVDKANVLQS SILWRETVTE MAKDYPEVTL EHIYIDNATM QLIKSPESFD
VLLCSNIFGD IISDEAAMIT GSMGMLPSAS LNEEGFGLYE PAGGSAPDIA GKGIANPIAQ
ILSAAMMLRY SFNLNEAADA IESAVQKVLA SGHRTADLAD DSTPVSTAEM GTLITQAI
