ID Q0VQ19_ALCBS Unreviewed; 740 AA. AC Q0VQ19; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 27-MAR-2024, entry version 102. 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:CAL16729.1}; GN OrderedLocusNames=ABO_1281 {ECO:0000313|EMBL:CAL16729.1}; OS Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 / OS SK2). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales; OC Alcanivoracaceae; Alcanivorax. OX NCBI_TaxID=393595 {ECO:0000313|EMBL:CAL16729.1, ECO:0000313|Proteomes:UP000008871}; RN [1] {ECO:0000313|EMBL:CAL16729.1, ECO:0000313|Proteomes:UP000008871} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2 RC {ECO:0000313|Proteomes:UP000008871}; RX PubMed=16878126; DOI=10.1038/nbt1232; RA Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M., RA Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C., RA Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B., RA McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O., RA Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J., RA Weidner S., Kaiser O., Golyshin P.N.; RT "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium RT Alcanivorax borkumensis."; RL Nat. Biotechnol. 24:997-1004(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: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; AM286690; CAL16729.1; -; Genomic_DNA. DR RefSeq; WP_011588564.1; NC_008260.1. DR AlphaFoldDB; Q0VQ19; -. DR STRING; 393595.ABO_1281; -. DR KEGG; abo:ABO_1281; -. DR eggNOG; COG2838; Bacteria. DR HOGENOM; CLU_025308_1_0_6; -. DR OrthoDB; 9807643at2; -. DR Proteomes; UP000008871; 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 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:CAL16729.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008871}; KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}. FT BINDING 82..87 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 132..139 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 135 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 145 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 350 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3" FT BINDING 547 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 548 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3" FT BINDING 552 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3" FT BINDING 584..585 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 589 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 600..602 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 649 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT SITE 255 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1" FT SITE 420 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1" SQ SEQUENCE 740 AA; 82598 MW; E93E9721F03991CC CRC64; MTTPKIIYTM TDEAPALATY SFLPIIEKFT SIAGIEVESS DISLATRILA SFPEYLSEQQ KVKDTLSELS DLTQDPEANI IKLPNISASI PQLREAIAEL NEHGYAVPEY PDEPQNEKEK DIQARYTKIL GSAVNPVLRE GNSDRRAPIA VKNYARKNPH SMGYWSPASR THVAHMRGGD FFSHETSCTI DKACKVRIEF EDSNGNITVK KPDLALLDGE VIDAMYMSKK ALCAFFDEQI EDAKNTGMLF SLHVKATMMK VSHPIVFGHA VRCFYRELFE KHGEILEKIG ANPNNGLSNI YQKIEELPIS QRLEIESTIR ACYLHRPELA MVDSDRGISN LHVPSDVIVD ASMPAMIRQG GKMYGADGKL KDTKAVIPES TYATIYQEVI NFCKTHGAFD PVTCGSVPNV GLMAQKAEEY GSHDKTFEAT ADGSMRIVRE DGEVLLTHKV EQGDIWRMCQ AKDLPIRDWV KLAVVRARLS NTPAIFWLDK ERAHDAQLIL KVKEYLKDHD TEGLDIRIMS PVQAIRYTME RMIRGKDTIS VTGNVLRDYL TDLFPILELG TSAKMLSIVP LMAGGGLYET GAGGSAPKHV QQFLEENHLR WDSLGEFLAL SVSIQELGEK YGNKKAKVIA AALDKANEQY LEQNKSPSRK VGQPDNRVSH FYVAMYWAQA LAAQDDDAEL KEKFTEIASS LSQNEEKIVK EMVAVQGSPI DIGGYYNPDF NKASQAMRPS GTFNQILEKL //