ID F2I0U8_PELSM Unreviewed; 404 AA. AC F2I0U8; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAR-2024, entry version 64. DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108}; DE EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108}; GN OrderedLocusNames=SAR11G3_00909 {ECO:0000313|EMBL:AEA81383.1}; OS Pelagibacter sp. (strain IMCC9063). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales; OC Candidatus Pelagibacteraceae; Pelagibacter. OX NCBI_TaxID=1002672 {ECO:0000313|EMBL:AEA81383.1, ECO:0000313|Proteomes:UP000009181}; RN [1] {ECO:0000313|EMBL:AEA81383.1, ECO:0000313|Proteomes:UP000009181} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMCC9063 {ECO:0000313|EMBL:AEA81383.1, RC ECO:0000313|Proteomes:UP000009181}; RX PubMed=21515764; DOI=10.1128/JB.05033-11; RA Oh H.M., Kang I., Lee K., Jang Y., Lim S.I., Cho J.C.; RT "Complete genome sequence of strain IMCC9063, belonging to SAR11 subgroup RT 3, isolated from the Arctic Ocean."; RL J. Bacteriol. 193:3379-3380(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; CP002511; AEA81383.1; -; Genomic_DNA. DR RefSeq; WP_013695548.1; NC_015380.1. DR AlphaFoldDB; F2I0U8; -. DR STRING; 1002672.SAR11G3_00909; -. DR KEGG; pel:SAR11G3_00909; -. DR eggNOG; COG0538; Bacteria. DR HOGENOM; CLU_023296_1_1_5; -. DR OrthoDB; 9765655at2; -. DR Proteomes; UP000009181; 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: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; 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. 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|PIRNR:PIRNR000108, ECO:0000256|PIRSR:PIRSR000108-4}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|PIRNR:PIRNR000108}; KW Reference proteome {ECO:0000313|Proteomes:UP000009181}; KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}. FT DOMAIN 9..395 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 251 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-3" FT BINDING 259 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4" FT BINDING 274 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-3" FT BINDING 309..314 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4" FT BINDING 327 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 211 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-1" SQ SEQUENCE 404 AA; 45793 MW; 18C44D8B65A72FF1 CRC64; MAKIKVKNPV VELDGDEMTR IIWEFIKNKL ILPYLDVELK YFDLGMESRD KTDDQITIDS ANEIKKYGVG VKCATITPDE ARVEEFKLKK MWKSPNGTIR NILGGTIFRE PIIMKNVPRL VPGWTDPIVI GRHAYGDQYR ATDFKVPGKG KLTVKWTSED GNDTVEHDVF DFPGSGIAMT MYNLDESIKD FARSCMNYGL LRKWPVYLST KNTILKTYDG RFKDLFQEIF DNEFKDEFAK HKLTYEHRLI DDMVACAMKW SGGYVWACKN YDGDVQCDTV AQGYGSLGLM TSVLMTPDGK TVESEAAHGT VTRHYREHQK GNETSTNPVA SIFAWTRGLA HRGKLDGNQE LIDFAHALEQ TCVETVETGE MTKDLAVLVG GEQKFLTTSQ FLEAINKNLQ SKLN //