IDH_HALVD
ID IDH_HALVD Reviewed; 419 AA.
AC D4GU92; Q8X277;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000303|PubMed:8593959};
DE Short=IDH {ECO:0000250|UniProtKB:P08200};
DE EC=1.1.1.42 {ECO:0000269|PubMed:12007799, ECO:0000269|PubMed:8593959};
DE AltName: Full=ICDH {ECO:0000303|PubMed:12007799};
DE AltName: Full=IDP {ECO:0000250|UniProtKB:P08200};
DE AltName: Full=NADP(+)-specific ICDH {ECO:0000250|UniProtKB:P08200};
DE AltName: Full=Oxalosuccinate decarboxylase {ECO:0000250|UniProtKB:P08200};
GN Name=icd {ECO:0000312|EMBL:ADE02810.1};
GN Synonyms=icdh {ECO:0000312|EMBL:CAC80860.2};
GN OrderedLocusNames=HVO_2588 {ECO:0000312|EMBL:ADE02810.1};
GN ORFNames=C498_08220 {ECO:0000312|EMBL:ELY32497.1};
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], CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=12007799; DOI=10.1111/j.1574-6968.2002.tb11125.x;
RA Camacho M., Rodriguez-Arnedo A., Bonete M.J.;
RT "NADP-dependent isocitrate dehydrogenase from the halophilic archaeon
RT Haloferax volcanii: cloning, sequence determination and overexpression in
RT Escherichia coli.";
RL FEMS Microbiol. Lett. 209:155-160(2002).
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).
RN [4]
RP PROTEIN SEQUENCE OF 2-19, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=8593959; DOI=10.1111/j.1574-6968.1995.tb07919.x;
RA Camacho M.L., Brown R.A., Bonete M.J., Danson M.J., Hough D.W.;
RT "Isocitrate dehydrogenases from Haloferax volcanii and Sulfolobus
RT solfataricus: enzyme purification, characterisation and N-terminal
RT sequence.";
RL FEMS Microbiol. Lett. 134:85-90(1995).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH;
CC Xref=Rhea:RHEA:19629, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.42;
CC Evidence={ECO:0000269|PubMed:12007799, ECO:0000269|PubMed:8593959};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P08200};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P08200};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC {ECO:0000250|UniProtKB:P08200};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=110 uM for NADP (for native enzyme) {ECO:0000269|PubMed:8593959};
CC KM=93 uM for NADP (for recombinant enzyme)
CC {ECO:0000269|PubMed:12007799};
CC KM=130 uM for isocitrate (for native enzyme)
CC {ECO:0000269|PubMed:8593959};
CC KM=105 uM for isocitrate (for recombinant enzyme)
CC {ECO:0000269|PubMed:12007799};
CC Vmax=68 umol/min/mg enzyme (for native enzyme)
CC {ECO:0000269|PubMed:8593959};
CC Vmax=77 umol/min/mg enzyme (for recombinant enzyme)
CC {ECO:0000269|PubMed:12007799};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8593959}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {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; AJ251585; CAC80860.2; -; Genomic_DNA.
DR EMBL; CP001956; ADE02810.1; -; Genomic_DNA.
DR EMBL; AOHU01000046; ELY32497.1; -; Genomic_DNA.
DR RefSeq; WP_004042658.1; NZ_AOHU01000046.1.
DR AlphaFoldDB; D4GU92; -.
DR SMR; D4GU92; -.
DR STRING; 309800.C498_08220; -.
DR EnsemblBacteria; ADE02810; ADE02810; HVO_2588.
DR EnsemblBacteria; ELY32497; ELY32497; C498_08220.
DR GeneID; 8926735; -.
DR KEGG; hvo:HVO_2588; -.
DR PATRIC; fig|309800.29.peg.1605; -.
DR eggNOG; arCOG01164; Archaea.
DR HOGENOM; CLU_031953_7_1_2; -.
DR OMA; CVRPCRY; -.
DR OrthoDB; 33452at2157; -.
DR BRENDA; 1.1.1.42; 2561.
DR SABIO-RK; D4GU92; -.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) 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:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004439; Isocitrate_DH_NADP_dimer_prok.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR PANTHER; PTHR43504; PTHR43504; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR TIGRFAMs; TIGR00183; prok_nadp_idh; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glyoxylate bypass; Magnesium; Manganese;
KW Metal-binding; NADP; Oxidoreductase; Reference proteome;
KW Tricarboxylic acid cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8593959"
FT CHAIN 2..419
FT /note="Isocitrate dehydrogenase [NADP]"
FT /id="PRO_0000431518"
FT BINDING 102
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08200"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P08200"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P08200"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P08200"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P08200"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P08200"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P08200"
FT BINDING 338..344
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08200"
FT BINDING 351
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08200"
FT BINDING 390
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08200"
FT BINDING 394
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08200"
FT SITE 158
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250|UniProtKB:P08200"
FT SITE 228
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250|UniProtKB:P08200"
FT CONFLICT 268
FT /note="E -> K (in Ref. 1; CAC80860)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="D -> N (in Ref. 1; CAC80860)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="E -> K (in Ref. 1; CAC80860)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="A -> T (in Ref. 1; CAC80860)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 45810 MW; 7D8913E0DFAC4980 CRC64;
MSYDQIEVPD DGEKITVDEE TGELSVPDNP IIPIIHGDGI GTDVGPAAQK VLDAAAEATG
RSVSWMRVYA GSSARDKYDE NLPEDTVSAI RNHRVAIKGP LTTPVGAGFR SLNVALRKKL
DLYANVRPTY HLDGVPSPVK NPSAMDMVTF RENTEDVYAG IEWEAGTDEV QKVKEFVEEE
MGADGVIHDG PVGIGIKPIT EFGTKRLVRE AIEYALENDR PSVTLVHKGN IMKFTEGAFR
DWGYELAEEE FGDVTITEDE LWEEYDGERP EDKVVVKDRI ADNMLQQLLT RTADYDVIAT
MNLNGDYMSD AAGAQIGGLG IAPGANFGEG LCLAEPVHGS APKYAGEDKV NPTAMILSGR
LMFEYMGWKD AGKLIRDAVE KTISDGDVTY DLERQIEGGN KLATSEYADK VVENIKELA
