ID F9ZRS3_ACICS Unreviewed; 424 AA. AC F9ZRS3; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 02-SEP-2026, entry version 62. DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|RuleBase:RU004446}; DE EC=1.1.1.42 {ECO:0000256|RuleBase:RU004446}; GN OrderedLocusNames=Atc_2440 {ECO:0000313|EMBL:AEK59088.1}; OS Acidithiobacillus caldus (strain SM-1). OC Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia; OC Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus. OX NCBI_TaxID=990288 {ECO:0000313|EMBL:AEK59088.1, ECO:0000313|Proteomes:UP000006135}; RN [1] {ECO:0000313|EMBL:AEK59088.1, ECO:0000313|Proteomes:UP000006135} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM-1 {ECO:0000313|EMBL:AEK59088.1, RC ECO:0000313|Proteomes:UP000006135}; RX PubMed=21703548; DOI=10.1016/j.jgg.2011.04.006; RA You X.Y., Guo X., Zheng H.J., Zhang M.J., Liu L.J., Zhu Y.Q., Zhu B., RA Wang S.Y., Zhao G.P., Poetsch A., Jiang C.Y., Liu S.J.; RT "Unraveling the Acidithiobacillus caldus complete genome and its central RT metabolisms for carbon assimilation."; RL J. Genet. Genomics 38:243-252(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|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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}. 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; CP002573; AEK59088.1; -; Genomic_DNA. DR RefSeq; WP_004868721.1; NC_015850.1. DR AlphaFoldDB; F9ZRS3; -. DR STRING; 990288.Atc_2440; -. DR GeneID; 92932350; -. DR KEGG; acu:Atc_2440; -. DR HOGENOM; CLU_031953_7_1_6; -. DR OrthoDB; 5287711at2; -. DR Proteomes; UP000006135; Chromosome. DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule. 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 NCBIfam; NF005425; PRK07006.1; 1. DR NCBIfam; TIGR00183; prok_nadp_idh; 1. 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 ECO:0000256|RuleBase:RU004446}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR604439-3}; KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRSR:PIRSR604439-3}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|RuleBase:RU004446}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR604439-2}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Reference proteome {ECO:0000313|Proteomes:UP000006135}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, KW ECO:0000256|RuleBase:RU004446}. FT DOMAIN 21..418 FT /note="Isopropylmalate dehydrogenase-like" FT /evidence="ECO:0000259|SMART:SM01329" FT BINDING 106 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 108 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 112 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 122 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 146 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 313 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-3" FT BINDING 358 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT SITE 153 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4" FT SITE 223 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4" FT MOD_RES 93 FT /note="N6-succinyllysine" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5" FT MOD_RES 106 FT /note="Phosphoserine" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5" SQ SEQUENCE 424 AA; 45501 MW; C6ECB6ABE0389E92 CRC64; MSGGSLIRWA AGRLEVPDRP IIPFIEGDGI GVDVTPAMRR VVDAAVAKAY GGARAIVWRE LLAGQKAVAE LGADQILPEA TLAAIREHHV AIKGPLETPV GTGMRSLNVA LRQELDLYVC QRPVRYFRGT PSPLREPEKV DMVIFRENSE DIYAGIEWPA ESPEARRLIA FLREEMGVRK IRFPESSAIG IKPVSREGSE RLIRRAIAYA LAQGKPSVTL VHKGNIMKFT EGGFRDWGYA LAEREFGEQV FTWRQKTALA KSEGKAAAEA AEKAAVAAGK LIVKDVIADN FLQQILLRPE LYSVVATLNL NGDYLSDALA AEVGGIGMAP GANLSDSHAI FEATHGTAPD IAGLGRANPS SLILSAVMLL EHIGWPEAAE RILAAMEATI GAGEVTADLA ALRGDVPALS TAEFTAALCR RVEA //