ID D3SQ42_THEAH Unreviewed; 419 AA. AC D3SQ42; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 27-MAR-2024, entry version 68. DE RecName: Full=isocitrate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00013013}; DE EC=1.1.1.42 {ECO:0000256|ARBA:ARBA00013013}; GN OrderedLocusNames=Thal_0646 {ECO:0000313|EMBL:ADC89279.1}; OS Thermocrinis albus (strain DSM 14484 / JCM 11386 / HI 11/12). OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Thermocrinis. OX NCBI_TaxID=638303 {ECO:0000313|EMBL:ADC89279.1, ECO:0000313|Proteomes:UP000002043}; RN [1] {ECO:0000313|Proteomes:UP000002043} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14484 / JCM 11386 / HI 11/12 RC {ECO:0000313|Proteomes:UP000002043}; RX DOI=10.4056/sigs.761490; RA Wirth R., Sikorski J., Brambilla E., Misra M., Lapidus A., Copeland A., RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C., RA Tapia R., Bruce D., Goodwin L., Pitluck S., Pati A., Anderson I., RA Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K., RA Bilek Y., Hader T., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Tindall B.J., Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Thermocrinis albus type strain (HI 11/12T)."; RL Stand. Genomic Sci. 2:194-202(2010). 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 -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}. 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; CP001931; ADC89279.1; -; Genomic_DNA. DR RefSeq; WP_012991686.1; NC_013894.1. DR AlphaFoldDB; D3SQ42; -. DR STRING; 638303.Thal_0646; -. DR KEGG; tal:Thal_0646; -. DR eggNOG; COG0538; Bacteria. DR HOGENOM; CLU_031953_7_1_0; -. DR OrthoDB; 9806254at2; -. DR Proteomes; UP000002043; 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: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; 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 PROSITE; PS00470; IDH_IMDH; 1. PE 3: Inferred from homology; KW Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR604439-3}; KW Manganese {ECO:0000256|PIRSR:PIRSR604439-3}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR604439-2}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Reference proteome {ECO:0000313|Proteomes:UP000002043}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}. FT DOMAIN 36..415 FT /note="Isopropylmalate dehydrogenase-like" FT /evidence="ECO:0000259|SMART:SM01329" FT BINDING 119 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 121 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 125 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 135 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 158 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 306 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-3" FT BINDING 351 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT BINDING 398 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT SITE 165 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4" FT SITE 235 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4" FT MOD_RES 106 FT /note="N6-succinyllysine" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5" FT MOD_RES 119 FT /note="Phosphoserine" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5" SQ SEQUENCE 419 AA; 46060 MW; 7A762876777E6A81 CRC64; MLERVYRWEG KAVLPQEGSF IKLLPDKRIE VPHNPIIPFI EGDGIGPEIA PAMILVVNRA VEKAYGGSRL IYWVELLAGD KAEALTGKRM PEETLEVLKE AVVSIKGPLG TPVGKGGKSL NAILRQSMDF YSAIRPVYWL GQPAPIPEPH RVNVTVFREN SDDVYMGIEY MPGSQDTQKV RKFFLEEMGV SPYALPEDCG ITVKPMSEYK TKRHVRKALR YALEKGLKVV AVVGKGNIMK ATEGAFMNWA FEVAKEPEFE GRVITEGEPK DGQVLLTRVI TDQMLMQLVL KPEAYHVIIT QNLNGDYISD LAAALVGGPG FVPSGNIGDG YALFESTHGT AYDIAGKNIA NPLSLTLSGA MMLEYLGWKE AAQLIYDAVK KAIEDRLGTP DIAKGFEKMG VEAKALSTME FAQAIAERI //