ID IDH2_COLMA Reviewed; 743 AA. AC P41561; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 14-APR-2009, sequence version 3. DT 02-SEP-2026, entry version 95. DE RecName: Full=Isocitrate dehydrogenase [NADP] 2; DE EC=1.1.1.42 {ECO:0000305|PubMed:3129416}; DE AltName: Full=IDH-II {ECO:0000303|PubMed:3129416}; DE AltName: Full=IDP-2; DE AltName: Full=NADP(+)-specific ICDH 2; DE AltName: Full=Oxalosuccinate decarboxylase 2; GN Name=icd2; Synonyms=icdII {ECO:0000303|PubMed:8226630}; OS Colwellia maris. OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Alteromonadales; Colwelliaceae; Colwellia. OX NCBI_TaxID=77524; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8226630; DOI=10.1128/jb.175.21.6873-6880.1993; RA Ishii A., Suzuki M., Sahara T., Takada Y., Sasaki S., Fukunaga N.; RT "Genes encoding two isocitrate dehydrogenase isozymes of a psychrophilic RT bacterium, Vibrio sp. strain ABE-1."; RL J. Bacteriol. 175:6873-6880(1993). RN [2] RP SEQUENCE REVISION TO 660-673. RA Ishii A., Suzuki M., Sahara T., Takada Y., Sasaki S., Fukunaga N.; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. RN [3] RP PROTEIN SEQUENCE OF 2-39. RX PubMed=1295895; DOI=10.1093/oxfordjournals.jbchem.a123988; RA Fukunaga N., Imagawa S., Sahara T., Ishii A., Suzuki M.; RT "Purification and characterization of monomeric isocitrate dehydrogenase RT with NADP(+)-specificity from Vibrio parahaemolyticus Y-4."; RL J. Biochem. 112:849-855(1992). RN [4] RP PROTEIN SEQUENCE OF 2-14, AND SUBUNIT. RX PubMed=3129416; DOI=10.1093/oxfordjournals.jbchem.a122196; RA Ishii A., Ochiai T., Imagawa S., Fukunaga N., Sasaki S., Minowa O., RA Mizuno Y., Shiokawa H.; RT "Isozymes of isocitrate dehydrogenase from an obligately psychrophilic RT bacterium, Vibrio sp. strain ABE-1: purification, and modulation of RT activities by growth conditions."; RL J. Biochem. 102:1489-1498(1987). CC -!- FUNCTION: Catalyzes the oxidative decarboxylation of isocitrate to 2- CC oxoglutarate and carbon dioxide with the concomitant reduction of CC NADP(+). {ECO:0000305|PubMed:3129416}. 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:0000305|PubMed:3129416}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P50216}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000250|UniProtKB:P50216}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. CC {ECO:0000250|UniProtKB:P50216}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:3129416}. CC -!- SIMILARITY: Belongs to the monomeric-type IDH family. {ECO:0000305}. 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; D14047; BAA03134.2; -; Genomic_DNA. DR PIR; A49341; A49341. DR AlphaFoldDB; P41561; -. DR SMR; P41561; -. DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 2. DR InterPro; IPR004436; Isocitrate_DH_NADP_mono. DR NCBIfam; TIGR00178; monomer_idh; 1. DR PANTHER; PTHR36999:SF1; ISOCITRATE DEHYDROGENASE (NADP(+)); 1. DR PANTHER; PTHR36999; ISOCITRATE DEHYDROGENASE [NADP]; 1. DR Pfam; PF03971; IDH; 1. DR PIRSF; PIRSF009407; IDH_monmr; 1. DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Glyoxylate bypass; Magnesium; Manganese; KW Metal-binding; NADP; Oxidoreductase; Tricarboxylic acid cycle. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:1295895, FT ECO:0000269|PubMed:3129416" FT CHAIN 2..743 FT /note="Isocitrate dehydrogenase [NADP] 2" FT /id="PRO_0000083596" FT BINDING 87 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 89 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 134 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 137 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 137 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 141 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 147 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 257 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 352 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P50216" FT BINDING 422 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 549 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 550 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P50216" FT BINDING 554 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P50216" FT BINDING 587 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 591 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 602 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 604 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 651 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P16100" SQ SEQUENCE 743 AA; 80882 MW; DE1E71FF4B5A6E06 CRC64; MSTDNSKIIY TITDEAPALA TYSLLPIIQA YTASSGINVE TRDISLAGRI LANFPKYLTK EQRIDDALAE LGELAQTPEA NIIKLPNISA SIPQLEAVIK ELQAKGYDLP HYPAEPQNEA EESIKLTYAK ILGSAVNPVL REGNSDRRAP ASVKQYARNN PHSMGAWSKE SKSHVAHMAS GDFYGSEKSV TIDGATSVNI EFVAKNGDVT LLKSKLPLLD KEIIDASVMS KSALVEFFET EINKAKEEDV LLSLHLKATM MKVSDPVMFG HAVRVFYKDV FAKHAATFEQ LGVDADNGIG DVYAKIARLP AAQKEEIEAD LQAVYATRPE MAMVDSDKGI TNLHVPSDVI IDASMPAALR ASGMMWGPDG KQKDTKFMIP DRNYAGVFSA VVDFCRENGA FNPATMGTVP NVGLMAQKAE EYGSHDKTFT MKAAGTVRVV NSQGERLIEQ EVAQGDIYRM CQVKDAPIQD WVKLAVTRAR ATGTPTVFWL DENRGHDEQM IKKVNTYLAD HDTTGLDIQI LEPVKACEFT LARVAKGEDA ISVTGNVLRD YLTDLFPILE LGTSAKMLSI VPLMNGGGLF ETGAGGSAPK HVQQFEKENH LRWDSLGEFL ALAASLEHVA VTTGNARAQI LADTLDAATG KFLDTNKSPS RKVGELDNRG SHFYLAMYWA QALAAQTTDT ELQASFSSVA QALTKQEEKI VAELNAAQGP AIDLNGYYFA DTKLAEKAMR PSETFNTILS ALL //