ID Q9X0N2_THEMA Unreviewed; 399 AA.
AC Q9X0N2; G4FEJ9;
DT 01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 152.
DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN OrderedLocusNames=TM_1148 {ECO:0000313|EMBL:AAD36224.1};
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Thermotoga.
OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36224.1, ECO:0000313|Proteomes:UP000008183};
RN [1] {ECO:0000313|EMBL:AAD36224.1, ECO:0000313|Proteomes:UP000008183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8
RC {ECO:0000313|Proteomes:UP000008183};
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., Heidelberg J.,
RA Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., Smith H.O.,
RA Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2] {ECO:0007829|PDB:1ZOR}
RP X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS).
RX PubMed=16759231; DOI=10.1111/j.1742-4658.2006.05298.x;
RA Karlstrom M., Steen I.H., Madern D., Fedoy A.E., Birkeland N.K.,
RA Ladenstein R.;
RT "The crystal structure of a hyperthermostable subfamily II isocitrate
RT dehydrogenase from Thermotoga maritima.";
RL FEBS J. 273:2851-2868(2006).
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:0000256|PIRNR:PIRNR000108};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRNR:PIRNR000108,
CC ECO:0000256|PIRSR:PIRSR000108-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRNR:PIRNR000108,
CC ECO:0000256|PIRSR:PIRSR000108-3};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC {ECO:0000256|PIRNR:PIRNR000108, ECO:0000256|PIRSR:PIRSR000108-3};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769,
CC ECO:0000256|PIRNR:PIRNR000108}.
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DR EMBL; AE000512; AAD36224.1; -; Genomic_DNA.
DR PIR; H72288; H72288.
DR RefSeq; NP_228954.1; NC_000853.1.
DR RefSeq; WP_004080233.1; NZ_CP011107.1.
DR PDB; 1ZOR; X-ray; 2.24 A; A/B=1-399.
DR PDBsum; 1ZOR; -.
DR AlphaFoldDB; Q9X0N2; -.
DR SMR; Q9X0N2; -.
DR PaxDb; 243274-THEMA_08600; -.
DR EnsemblBacteria; AAD36224; AAD36224; TM_1148.
DR KEGG; tma:TM1148; -.
DR KEGG; tmw:THMA_1172; -.
DR PATRIC; fig|243274.17.peg.1153; -.
DR InParanoid; Q9X0N2; -.
DR OrthoDB; 9765655at2; -.
DR BRENDA; 1.1.1.42; 6331.
DR EvolutionaryTrace; Q9X0N2; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006102; P:isocitrate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR004790; Isocitrate_DH_NADP.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR NCBIfam; TIGR00127; nadp_idh_euk; 1.
DR PANTHER; PTHR11822:SF21; ISOCITRATE DEHYDROGENASE [NADP], MITOCHONDRIAL; 1.
DR PANTHER; PTHR11822; NADP-SPECIFIC ISOCITRATE DEHYDROGENASE; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR PIRSF; PIRSF000108; IDH_NADP; 1.
DR SMART; SM01329; Iso_dh; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:1ZOR};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000108};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRNR:PIRNR000108};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000108}; NADP {ECO:0000256|PIRNR:PIRNR000108};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000108};
KW Reference proteome {ECO:0000313|Proteomes:UP000008183};
KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}.
FT DOMAIN 9..391
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
FT BINDING 77
FT /ligand="D-threo-isocitrate"
FT /ligand_id="ChEBI:CHEBI:15562"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT BINDING 94..100
FT /ligand="D-threo-isocitrate"
FT /ligand_id="ChEBI:CHEBI:15562"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT BINDING 109
FT /ligand="D-threo-isocitrate"
FT /ligand_id="ChEBI:CHEBI:15562"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT BINDING 132
FT /ligand="D-threo-isocitrate"
FT /ligand_id="ChEBI:CHEBI:15562"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT BINDING 247
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-3"
FT BINDING 270
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-3"
FT SITE 139
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-1"
FT SITE 208
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-1"
SQ SEQUENCE 399 AA; 45403 MW; 21828AFA6AE10034 CRC64;
MEKVKVKNPI VELDGDEMAR VMWKMIKEKL ILPYLDIQLV YFDLGIKKRD ETDDQITIEA
AKAIKKYGVG VKCATITPDA ERVKEYNLKK AWKSPNATIR AYLDGTVFRK PIMVKNVPPL
VKRWKKPIII GRHAYGDIYN AVEAKVEGPA EVELVVRNKE NKTLLVHKFE GNGVVMAMHN
LEKSIRSFAQ SCINYAISEK VDIWFATKDT ISKVYHAYFK DIFQEEVDKR KEELEKAGVN
YRYMLIDDAA AQILRSEGGM LWACMNYEGD IMSDMIASGF GSLGLMTSVL VSPDGVYEFE
AAHGTVRRHY YRYLKGEKTS TNPTASIFAW TGAIRKRGEL DGTPEVCEFA DKLEKAVINT
IESGVITKDL QPFTEPPIDK YVTLEEFIDE VKKNLEKLL
//
