ID A0A256Y0P3_9EURY Unreviewed; 411 AA. AC A0A256Y0P3; DT 22-NOV-2017, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 1. DT 28-JUN-2023, entry version 14. DE RecName: Full=isocitrate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00013013}; DE EC=1.1.1.42 {ECO:0000256|ARBA:ARBA00013013}; GN ORFNames=B6U96_14045 {ECO:0000313|EMBL:OYT34023.1}; OS Archaeoglobales archaeon ex4484_92. OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales. OX NCBI_TaxID=2012529 {ECO:0000313|EMBL:OYT34023.1, ECO:0000313|Proteomes:UP000216673}; RN [1] {ECO:0000313|Proteomes:UP000216673} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Dombrowski N., Seitz K.W., Teske A., Baker B.; RT "Novel pathways for hydrocarbon cycling and metabolic interdependencies in RT hydrothermal sediment communities."; RL Submitted (JUN-2017) 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|ARBA:ARBA00023554}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR604439-3}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRSR:PIRSR604439-3}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. CC {ECO:0000256|PIRSR:PIRSR604439-3}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|ARBA:ARBA00001936}; CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:OYT34023.1}. 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; NJDI01000193; OYT34023.1; -; Genomic_DNA. DR AlphaFoldDB; A0A256Y0P3; -. DR Proteomes; UP000216673; Unassembled WGS sequence. 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:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1. DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS. DR InterPro; IPR004439; Isocitrate_DH_NADP_dimer_prok. DR InterPro; IPR024084; IsoPropMal-DH-like_dom. DR PANTHER; PTHR43504; ISOCITRATE DEHYDROGENASE [NADP]; 1. DR PANTHER; PTHR43504:SF1; ISOCITRATE DEHYDROGENASE [NADP]; 1. DR Pfam; PF00180; Iso_dh; 1. DR SMART; SM01329; Iso_dh; 1. DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1. DR TIGRFAMs; TIGR00183; prok_nadp_idh; 1. DR PROSITE; PS00470; IDH_IMDH; 1. PE 4: Predicted; KW Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435}; KW Magnesium {ECO:0000256|PIRSR:PIRSR604439-3}; KW Manganese {ECO:0000256|PIRSR:PIRSR604439-3}; KW NADP {ECO:0000256|PIRSR:PIRSR604439-2}; KW Oxidoreductase {ECO:0000313|EMBL:OYT34023.1}. FT DOMAIN 28..404 FT /note="Isopropylmalate dehydrogenase-like" FT /evidence="ECO:0000259|SMART:SM01329" FT BINDING 99 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT BINDING 108 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 110 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 114 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 124 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 148 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 300 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-3" FT BINDING 332..338 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT BINDING 345 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT BINDING 384 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT BINDING 388 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT SITE 155 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4" FT SITE 222 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4" FT MOD_RES 95 FT /note="N6-succinyllysine" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5" FT MOD_RES 108 FT /note="Phosphoserine" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5" SQ SEQUENCE 411 AA; 45969 MW; 73B7138AE8C23716 CRC64; MYQKIVPPKD GEKIIFADDK LKVPDNPIIP YIVGDGIGKD VVPAAIKVID AAVKRIGKEI IWFRVYAGED AFKLYGNYLP QDTIDAIREF RVALKGPLTT PIGTGYRSLN VTLRQILDLY ANVRPIYYIE GIPSPINHPE KVNFVIFREN TEDVYSGIEF ERGSTEAIKL KKFLSEEFGI HIRDDAGIGI KPISEFATKR LVRMAIKYAI ENKRQSVTLV HKGNIMKYTE GAFRDWGYEV AIQEFGDYCI TEQELYQNYD GIRPKNKIVI KDRIADNMFQ QILTRTEEYD VIALPNLNGD YLSDAAAALI GGLGVAPGSN IGDGIGVFEP IHGSAPKYTG LGKVNPTAEI LTGCLMLEYI GWKEASDLIK RAIQMTIKDR IVTYDIHRHT GGKLVGTMEF ANAVIDNLET L //