ID F2JWD6_MARM1 Unreviewed; 739 AA. AC F2JWD6; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAR-2024, entry version 62. DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR009407}; DE EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR009407}; DE AltName: Full=Oxalosuccinate decarboxylase {ECO:0000256|PIRNR:PIRNR009407}; GN OrderedLocusNames=Marme_1336 {ECO:0000313|EMBL:ADZ90609.1}; OS Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 / OS MMB-1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales; OC Oceanospirillaceae; Marinomonas. OX NCBI_TaxID=717774 {ECO:0000313|EMBL:ADZ90609.1, ECO:0000313|Proteomes:UP000001062}; RN [1] {ECO:0000313|EMBL:ADZ90609.1, ECO:0000313|Proteomes:UP000001062} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1 RC {ECO:0000313|Proteomes:UP000001062}; RX PubMed=22675599; DOI=10.4056/sigs.2545743; RA Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C., RA Detter J.C., Copeland A., Teshima H., Bruce D., Detter C., Tapia R., RA Han S., Land M.L., Ivanova N., Mikhailova N., Johnston A.W., RA Sanchez-Amat A.; RT "Complete genome sequence of the melanogenic marine bacterium Marinomonas RT mediterranea type strain (MMB-1(T))."; RL Stand. Genomic Sci. 6:63-73(2012). 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:PIRNR009407}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR009407-3}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRSR:PIRSR009407-3}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. CC {ECO:0000256|PIRSR:PIRSR009407-3}; CC -!- SIMILARITY: Belongs to the monomeric-type IDH family. CC {ECO:0000256|PIRNR:PIRNR009407}. 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; CP002583; ADZ90609.1; -; Genomic_DNA. DR RefSeq; WP_013660514.1; NZ_CP047696.1. DR AlphaFoldDB; F2JWD6; -. DR STRING; 717774.Marme_1336; -. DR KEGG; mme:Marme_1336; -. DR PATRIC; fig|717774.3.peg.1384; -. DR eggNOG; COG2838; Bacteria. DR HOGENOM; CLU_025308_1_0_6; -. DR OrthoDB; 9807643at2; -. DR Proteomes; UP000001062; 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:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR InterPro; IPR004436; Isocitrate_DH_NADP_mono. DR NCBIfam; TIGR00178; monomer_idh; 1. DR PANTHER; PTHR36999; ISOCITRATE DEHYDROGENASE [NADP]; 1. DR PANTHER; PTHR36999:SF1; ISOCITRATE DEHYDROGENASE [NADP]; 1. DR Pfam; PF03971; IDH; 1. DR PIRSF; PIRSF009407; IDH_monmr; 1. DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1. PE 3: Inferred from homology; KW Glyoxylate bypass {ECO:0000256|PIRNR:PIRNR009407}; KW Magnesium {ECO:0000256|PIRSR:PIRSR009407-3}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR009407-3}; KW NADP {ECO:0000256|PIRNR:PIRNR009407, ECO:0000256|PIRSR:PIRSR009407-4}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR009407, KW ECO:0000313|EMBL:ADZ90609.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001062}; KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}. FT BINDING 82..87 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 132..139 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 135 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 145 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 349 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3" FT BINDING 546 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 547 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3" FT BINDING 551 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3" FT BINDING 583..584 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 588 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 599..601 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 648 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT SITE 254 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1" FT SITE 419 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1" SQ SEQUENCE 739 AA; 82315 MW; E7DAF5E2241CCA22 CRC64; MSKHTIYYTL TDEAPALATA SLLPIFQAFA KEADINLQLT DISLAARVLS LFTDRLPEDK QVEDGLSFLG ELTADPDANF IKLPNISASI PQLTATIKEL QSQGYEIPDY PEAPATDEEK EINSRYSKVL GSAVNPVLRQ GNSDRRAPAA VKGFARKHPH SMGKWQKTSQ THADYMRDGD FFSSEQSVTM DKAQEVRIEF VNKSGEVDVK KTLPLLEGEV LDGMRMSASK LRDFFEQSLQ EAKEAGIMWS LHVKATMMKV SHPIVFGHAV TVYYKEVWDK FGDLFDELGV NPNNGIGSVY DKIKTLPQST QDEILESIHD CYEHRPEIAM VDSVRGITNL HVPSDVIVDA SMPAMIRSSG KMWGRDGKTK DTKAVMPEST YARIYQEVIN FCKTNGAFDP TTMGTVPNVG LMAQKAEEYG SHDKTFEVQE NGTMRVRDAE GNVLMQHDVE KGDIWRACQT KDAPIKDWVK LGVTRARNSG TPAVFWLDAE RAHDNELRKK VKLYLQDHDL EGLEIHIMSY NEAIRFSMER MMRGQDTISV SGNVLRDYLT DLFPIMELGT SAKMLSIVPM LNGGGMYETG AGGSAPKHVQ QLQEENYLRW DSLGEFLATA VSFEELGIKQ DNAKAKVLAA ALDRATEQLL DNNKSPSRKV GDIDNRGSHF YLTMYWAQAL ATQTDDAELA DKFASVAKAL VENESKIVEE LNSVQGKDAG LEGYYHMDLD AVTKVMRPSA TFNEILAAI //