ID C6XG72_LIBAP Unreviewed; 412 AA. AC C6XG72; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 27-MAR-2024, entry version 85. DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108}; DE EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108}; GN OrderedLocusNames=CLIBASIA_04005 {ECO:0000313|EMBL:ACT57375.1}; OS Liberibacter asiaticus (strain psy62). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Liberibacter. OX NCBI_TaxID=537021 {ECO:0000313|EMBL:ACT57375.1, ECO:0000313|Proteomes:UP000002744}; RN [1] {ECO:0000313|EMBL:ACT57375.1, ECO:0000313|Proteomes:UP000002744} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=psy62 {ECO:0000313|Proteomes:UP000002744}; RX PubMed=19589076; DOI=10.1094/MPMI-22-8-1011; RA Duan Y., Zhou L., Hall D.G., Li W., Doddapaneni H., Lin H., Liu L., RA Vahling C.M., Gabriel D.W., Williams K.P., Dickerman A., Sun Y., RA Gottwald T.; RT "Complete genome sequence of citrus huanglongbing bacterium, 'Candidatus RT Liberibacter asiaticus' obtained through metagenomics."; RL Mol. Plant Microbe Interact. 22:1011-1020(2009). RN [2] {ECO:0000313|EMBL:ACT57375.1, ECO:0000313|Proteomes:UP000002744} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=psy62 {ECO:0000313|Proteomes:UP000002744}; RX PubMed=21784907; DOI=10.1128/AEM.05111-11; RA Zhou L., Powell C.A., Hoffman M.T., Li W., Fan G., Liu B., Lin H., Duan Y.; RT "Diversity and plasticity of the intracellular plant pathogen and insect RT symbiont, 'Candidatus Liberibacter asiaticus', revealed by hyper variable RT prophage genes with intragenic tandem repeats."; RL Appl. Environ. Microbiol. 77:6663-6673(2011). 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}. 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; CP001677; ACT57375.1; -; Genomic_DNA. DR RefSeq; WP_015452733.1; NC_012985.3. DR AlphaFoldDB; C6XG72; -. DR STRING; 537021.CLIBASIA_04005; -. DR GeneID; 66286373; -. DR KEGG; las:CLIBASIA_04005; -. DR eggNOG; COG0538; Bacteria. DR HOGENOM; CLU_023296_1_1_5; -. DR OrthoDB; 9765655at2; -. DR Proteomes; UP000002744; Chromosome. 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: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; IPR019818; IsoCit/isopropylmalate_DH_CS. 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. DR PROSITE; PS00470; IDH_IMDH; 1. PE 3: Inferred from homology; 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}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000108}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|PIRNR:PIRNR000108}; KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}. FT DOMAIN 9..394 FT /note="Isopropylmalate dehydrogenase-like" FT /evidence="ECO:0000259|SMART:SM01329" FT BINDING 75..77 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4" FT BINDING 77 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2" FT BINDING 82 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4" 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 250 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-3" FT BINDING 258 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4" FT BINDING 273 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-3" FT BINDING 308..313 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4" FT BINDING 326 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4" FT SITE 139 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-1" FT SITE 210 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-1" SQ SEQUENCE 412 AA; 46577 MW; 65D6307019BC3244 CRC64; MKKIKVTKPV VSLDGDEMTR IIWQLIQENL IHPYLDIKIE YFDLSIQNRD LTDDQVTIDA AHAIKNCGVG IKCATITADQ ARVKEFNLKK MWKSPNGTIR NILGGIIFRE PIICSNVPRL IPGWKKPIII GRHAFGDQYR ATDFQFPSKG KLILKFVGDD GQTIEKEVFD SPGSGIAMAM YNLDDSIRNF ARAAMQYALA RQLPLYLSTK DTILKSYDGR FKNIFNEIFE AEFKNQFDEL GITYTHRLID DMVASSIKWS GGYIWACKNY DGDVQSDIVA QGFGSLGLMT SVLITADGKT METEAAHGTV TRHYRQHQQG KETSTNSIAS IFAWTRGLLH RAKLDENAEL KKFAENLERV CIKTVEDGFM TKDLALLIGP EQDWLSTTDF IEKISDNLRD ALQKNLSISD KQ //