ID A0Q7T7_FRATN Unreviewed; 738 AA. AC A0Q7T7; DT 09-JAN-2007, integrated into UniProtKB/TrEMBL. DT 09-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 97. DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR009407}; DE EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR009407}; DE AltName: Full=Oxalosuccinate decarboxylase {ECO:0000256|PIRNR:PIRNR009407}; GN Name=icd {ECO:0000313|EMBL:ABK90302.1}; GN OrderedLocusNames=FTN_1434 {ECO:0000313|EMBL:ABK90302.1}; GN ORFNames=AW25_567 {ECO:0000313|EMBL:AJI61347.1}; OS Francisella tularensis subsp. novicida (strain U112). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=401614 {ECO:0000313|EMBL:ABK90302.1, ECO:0000313|Proteomes:UP000000762}; RN [1] {ECO:0000313|EMBL:ABK90302.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=U112 {ECO:0000313|EMBL:ABK90302.1}; RA Brittnacher M., Rohmer L., Zhou Y., Abmayr S., D'Argenio D., Bovee D., RA Chang J., Chen J., Drees B., Ernst R., Fong C., Forsman M., Gallagher L., RA Gallis B., Gillett W., Goodlett D., Guina T., Guenthner D., Haugen E., RA Hayden H., Jacobs M., Kang A., Larson Freeman T., Levy R., Lim R., RA Manoil C., Olson M.V., Radey M., Shaffer S., Svensson K., Taylor G., RA Wasnick M., Kaul R., Miller S.I.; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000000762} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=U112 {ECO:0000313|Proteomes:UP000000762}; RX PubMed=17550600; DOI=10.1186/gb-2007-8-6-r102; RA Rohmer L., Fong C., Abmayr S., Wasnick M., Larson Freeman T.J., Radey M., RA Guina T., Svensson K., Hayden H.S., Jacobs M., Gallagher L.A., Manoil C., RA Ernst R.K., Drees B., Buckley D., Haugen E., Bovee D., Zhou Y., Chang J., RA Levy R., Lim R., Gillett W., Guenthener D., Kang A., Shaffer S.A., RA Taylor G., Chen J., Gallis B., D'Argenio D.A., Forsman M., Olson M.V., RA Goodlett D.R., Kaul R., Miller S.I., Brittnacher M.J.; RT "Comparison of Francisella tularensis genomes reveals evolutionary events RT associated with the emergence of human pathogenic strains."; RL Genome Biol. 8:R102.1-R102.16(2007). RN [3] {ECO:0000313|EMBL:AJI61347.1, ECO:0000313|Proteomes:UP000031872} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=U112 {ECO:0000313|EMBL:AJI61347.1, RC ECO:0000313|Proteomes:UP000031872}; RX PubMed=25931589; RA Johnson S.L., Daligault H.E., Davenport K.W., Coyne S.R., Frey K.G., RA Koroleva G.I., Broomall S.M., Bishop-Lilly K.A., Bruce D.C., Chertkov O., RA Freitas T., Jaissle J., Ladner J.T., Rosenzweig C.N., Gibbons H.S., RA Palacios G.F., Redden C.L., Xu Y., Minogue T.D., Chain P.S.; RT "Genome sequencing of 18 francisella strains to aid in assay development RT and testing."; RL Genome Announc. 3:0-0(2015). 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:PIRNR009407}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR009407-3}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRSR:PIRSR009407-3}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. CC {ECO:0000256|PIRSR:PIRSR009407-3}; CC -!- SIMILARITY: Belongs to the monomeric-type IDH family. CC {ECO:0000256|PIRNR:PIRNR009407}. 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; CP000439; ABK90302.1; -; Genomic_DNA. DR EMBL; CP009633; AJI61347.1; -; Genomic_DNA. DR RefSeq; WP_011733711.1; NZ_CP009633.1. DR AlphaFoldDB; A0Q7T7; -. DR KEGG; ftn:FTN_1434; -. DR KEGG; ftx:AW25_567; -. DR Proteomes; UP000000762; Chromosome. DR Proteomes; UP000031872; 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:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1. DR InterPro; IPR004436; Isocitrate_DH_NADP_mono. DR NCBIfam; TIGR00178; monomer_idh; 1. DR PANTHER; PTHR36999; ISOCITRATE DEHYDROGENASE [NADP]; 1. DR PANTHER; PTHR36999:SF1; ISOCITRATE DEHYDROGENASE [NADP]; 1. DR Pfam; PF03971; IDH; 1. DR PIRSF; PIRSF009407; IDH_monmr; 1. DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1. PE 3: Inferred from homology; KW Glyoxylate bypass {ECO:0000256|PIRNR:PIRNR009407}; KW Magnesium {ECO:0000256|PIRSR:PIRSR009407-3}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR009407-3}; KW NADP {ECO:0000256|PIRNR:PIRNR009407, ECO:0000256|PIRSR:PIRSR009407-4}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR009407, KW ECO:0000313|EMBL:AJI61347.1}; KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}. FT BINDING 80..85 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 130..137 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 133 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 143 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 348 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3" FT BINDING 545 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 546 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3" FT BINDING 550 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3" FT BINDING 582..583 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 587 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 598..600 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 647 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT SITE 253 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1" FT SITE 418 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1" SQ SEQUENCE 738 AA; 82260 MW; FE75E8AF37698124 CRC64; MHKIFYTFTD EAPALATGSF LPIVESFTKV ADIELETKDI SLSARILANF NDYLTAEQKC SDDLAILGEL AKTPDANIIK LPNISASIPQ LTAAIKELQS KGYKIPDYPY EPKDDKEQEI KARYAKVLGS AVNPVLREGN SDRRVADAVK KYAEKHPHSM GEWTKDSKSH VASMSADDFY ANEKSYIVPK ATKVKIVHTD TKGTQTVLKD NLALEEKEII DATKISIKAL REFYKNEIAK AKKEGTLLSL HLKATMMKVS DPILFGHAVE IFFEDIFKKY AKEFKELCVN PRNGWGDAVE KIKQLPQELQ DKINADIEKV FAKQPDIAMV NSDKGITNLN VPSDVIIDAS MPAAIRSSGK MWNKDGKLQD MKAMIPDRCY AGVYAATIDF CKENGAFDVA TMGDVSNVGL MAKKAEEYGS HDKTFEIQAD GKVEVIDAEG NVIFEHQVEK GDIWRACQTK DIAVKDWVKL AVNRAKITQN PAIFWLDSKR AHDRNLIAKV NEYLTHHDTT GLDIQILSPV EATKYSLKRM KEGKNTISVT GNVLRDYLTD LFPILELGTS AKMLSIVPLL AGGGLFETGA GGSAPKHVEQ LIEENHLRWD SLGEFLALGA SLEDLAIKTR DAKIKVLAET LSQANKDFLD NDKSPRRKVG ELDTRGSHFY LAYYWVKALA EQTGNAELKA KFEPIYIELK ANKDKIVKEL NDAQGKKVDV GGYYHMDRVK LDAVMRPSKT FNTILAQI //