ID Q5QZT7_IDILO Unreviewed; 741 AA. AC Q5QZT7; DT 04-JAN-2005, integrated into UniProtKB/TrEMBL. DT 04-JAN-2005, sequence version 1. DT 27-MAR-2024, entry version 106. 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=IL1433 {ECO:0000313|EMBL:AAV82273.1}; OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Idiomarinaceae; Idiomarina. OX NCBI_TaxID=283942 {ECO:0000313|EMBL:AAV82273.1, ECO:0000313|Proteomes:UP000001171}; RN [1] {ECO:0000313|EMBL:AAV82273.1, ECO:0000313|Proteomes:UP000001171} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR RC {ECO:0000313|Proteomes:UP000001171}; RX PubMed=15596722; DOI=10.1073/pnas.0407638102; RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., RA Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.; RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina RT loihiensis reveals amino acid fermentation as a source of carbon and RT energy."; RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004). 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; AE017340; AAV82273.1; -; Genomic_DNA. DR RefSeq; WP_011234679.1; NC_006512.1. DR AlphaFoldDB; Q5QZT7; -. DR STRING; 283942.IL1433; -. DR KEGG; ilo:IL1433; -. DR eggNOG; COG2838; Bacteria. DR HOGENOM; CLU_025308_1_0_6; -. DR OrthoDB; 9807643at2; -. DR Proteomes; UP000001171; 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 Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1. 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 Reference proteome {ECO:0000313|Proteomes:UP000001171}; KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}. FT REGION 140..171 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 84..89 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 134..141 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 137 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 147 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 351 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3" FT BINDING 548 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 549 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3" FT BINDING 553 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3" FT BINDING 585..586 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 590 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 601..603 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 650 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT SITE 256 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1" FT SITE 421 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1" SQ SEQUENCE 741 AA; 82455 MW; 9EA88DA0DD15246E CRC64; MSTDKAKIIY TETDEAPRLA TYSFLPFIEA FTKAAGVSVE TRDISLAGRI ISQFPEYLTE EQRQSDALAE LGEMAKTAEA NIIKLPNISA SIPQMTACIK ELQNQGYKLP DYPFDPQTDE EKDVRSRYDK VKGSAVNPVL REGNSDRRAP SAVKNYAKKH PHRMGEWSKD SKSHVAHMNE GDFYGSEKSV TSASEDTFKI VFESNGEQKV LKESVPVLAG EVVDAATMSK KQLQAFFEKE TVAAKEQGVL LSLHLKATMM KVSDPIMFGH AVRVFYKDVL EKHADLMKEI EFDPSNGIGD LYSKLDKLTA EQRDAIEVDM NAVYAKQPEL AMVNSHKGIT NLHVPSDIII DASMPAMIRD SGKMWDTNDS QQDAKAMIPD RSYAGVYQET IDFCRENGAF DPATMGTVPN VGLMAQKAEE YGSHDKTFEI PANGVVKVFN KAGDVVFEHK VEEGDIWRMC QVKDAPIRDW VKLAVNRSRL SGMPAVFWLD SNRAHDAQLI KKVEEYLKEH DTDGLDIQIM APVEATRHTL QRVKEGKDTI SVTGNVLRDY LTDLFPILEL GTSAKMLSIV PLMNGGGLFE TGAGGSAPKH VQQFVEENHL RWDSLGEFLA LAASLEHLSR TFDNKRALVL ADSLDLATAK FLEENKSPSR KVGEIDNRGS HFYLAMYWAE ALANQNEDAE LKERFSKLFE KLSGNEQAII NELNEIQGVK VDIGGYYQPN TDKVSAAMRP CSVLNETLGS L //