ID F6ACB0_PSEF1 Unreviewed; 742 AA. AC F6ACB0; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAR-2024, entry version 58. 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 OrderedLocusNames=Psefu_2325 {ECO:0000313|EMBL:AEF22292.1}; OS Pseudomonas fulva (strain 12-X). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=743720 {ECO:0000313|EMBL:AEF22292.1, ECO:0000313|Proteomes:UP000000686}; RN [1] {ECO:0000313|EMBL:AEF22292.1, ECO:0000313|Proteomes:UP000000686} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12-X {ECO:0000313|Proteomes:UP000000686}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Pagani I., Davenport K., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Lcollab F.I., RA Woyke T.; RT "Complete sequence of Pseudomonas fulva 12-X."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. 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; CP002727; AEF22292.1; -; Genomic_DNA. DR RefSeq; WP_013791421.1; NC_015556.1. DR AlphaFoldDB; F6ACB0; -. DR STRING; 743720.Psefu_2325; -. DR KEGG; pfv:Psefu_2325; -. DR eggNOG; COG2838; Bacteria. DR HOGENOM; CLU_025308_1_0_6; -. DR OrthoDB; 9807643at2; -. DR Proteomes; UP000000686; 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:AEF22292.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000686}; KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}. FT BINDING 83..88 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 133..140 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 136 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 146 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 351 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3" FT BINDING 548 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 549 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3" FT BINDING 553 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3" FT BINDING 585..586 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 590 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 601..603 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 650 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT SITE 256 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1" FT SITE 421 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1" SQ SEQUENCE 742 AA; 80113 MW; D1EDD95F98694A49 CRC64; MTTRSKIIYT LTDEAPALAT YSLLPIVKAF TASSDIAVET RDISLAGRIL ALFPEFLTDA QKQGDHLAEL GALATTPEAN IIKLPNISAS VPQLKAAIKE LQSQGYALPD YPDADDSEQA RDIRSRYDKV KGSAVNPVLR EGNSDRRAPL SVKNYARKHP HKMGAWAADS KSHVAHMESG DFYGSEKAAL IDAKGSVKIE LIGADGSTTV LKEKTSVLAD EVLDCSVMSK KALRSFIAAQ IEDAKKQGVL FSVHLKATMM KVSDPIIFGQ IVAEFYKPAL EKHAAALQEA GFNLNNGIGD LYASIKKLPA DKQAEIEADI NAVYADRPAL AMVNSDKGIT NLHVPSDVIV DASMPAMIRD SGRMWNTAGE LQDAKAVIPD RCYAGIYQAV IEDCKANGAF NPTTMGSVPN VGLMAQKAEE YGSHDKTFQI QAAGVVRVSD ANGKVLMEQK VEEGDIFRMC QTKDAPIQDW VKLAVNRARL SNTPAVFWLD PARAHDAEMI KKVEKYLKDH DTSGLDIRIL APVDAIKFSL ARIREGKDTI SVTGNVLRDY LTDLFPIMEL GTSAKMLSIV PLMNGGGLFE TGAGGSAPKH VQQLVEENFL RWDSLGEFLA LAASLEHLGN TYDNPKALVL SKTLDQATGQ FLDNDKSPAR KVGGIDNRGS HFYLALYWAQ ALAAQSEDAA LKAQFAPLAK TLTDNEAKIV AELGAVQGKP ADIGGYYAPN KELTEKVMRP SATLNAALAS LA //