LEU3_HALVD
ID LEU3_HALVD Reviewed; 324 AA.
AC D4GYE8; Q7ZAG5;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=3-isopropylmalate dehydrogenase;
DE EC=1.1.1.85;
GN Name=leuB; OrderedLocusNames=HVO_1502; ORFNames=C498_11221;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DS2 / DS70;
RX PubMed=14766575; DOI=10.1128/aem.70.2.943-953.2004;
RA Allers T., Ngo H.-P., Mevarech M., Lloyd R.G.;
RT "Development of additional selectable markers for the halophilic archaeon
RT Haloferax volcanii based on the leuB and trpA genes.";
RL Appl. Environ. Microbiol. 70:943-953(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:0000269|PubMed:14766575}.
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: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Auxotrophic for leucine.
CC {ECO:0000269|PubMed:14766575}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
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DR EMBL; AJ571689; CAE00175.1; -; Genomic_DNA.
DR EMBL; CP001956; ADE04611.1; -; Genomic_DNA.
DR EMBL; AOHU01000090; ELY28260.1; -; Genomic_DNA.
DR RefSeq; WP_004043433.1; NC_013967.1.
DR AlphaFoldDB; D4GYE8; -.
DR SMR; D4GYE8; -.
DR STRING; 309800.C498_11221; -.
DR EnsemblBacteria; ADE04611; ADE04611; HVO_1502.
DR EnsemblBacteria; ELY28260; ELY28260; C498_11221.
DR GeneID; 8925731; -.
DR KEGG; hvo:HVO_1502; -.
DR PATRIC; fig|309800.29.peg.2138; -.
DR eggNOG; arCOG01163; Archaea.
DR HOGENOM; CLU_031953_0_1_2; -.
DR OMA; TCAHKAN; -.
DR OrthoDB; 33452at2157; -.
DR UniPathway; UPA00048; UER00072.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 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..324
FT /note="3-isopropylmalate dehydrogenase"
FT /id="PRO_0000428968"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 254..266
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 119
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT SITE 165
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 324 AA; 33724 MW; 37A555AC19D985CB CRC64;
MTEEIVVIPG DGIGAEVIPA AVDVLKAVGD FEFVEADAGD HVKEETGEAL PQETYDLAAE
ADATLFGAAG ETAADVILPL RTAVDSFVNV RPAKAYPGVD ALRPETDLVF LRENTEGVYS
GHEDRLSEDL STLTRVVTTS ASERLAEYAC DYVGGEGGSF QVAHKANVMR ETDGRFRDAA
VAVADERGVE TEEVLMDAFA TRVCLDPTQF DTIVCPNLAG DVLSDLAAGL VGGLGLLPSA
NIGPDAALFE PVHGSAPDIA GEGIANPAAT ILSAAMLLDY LDHEAEADRV RSAVEGVLAD
GPRTPDLGGD ASTEDVTAAI LDRL
