ID   C7RB77_KANKD            Unreviewed;       740 AA.
AC   C7RB77;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   02-SEP-2026, entry version 87.
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=Kkor_1100 {ECO:0000313|EMBL:ACV26519.1};
OS   Kangiella koreensis (strain DSM 16069 / JCM 12317 / KCTC 12182 / SW-125).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Kangiellales; Kangiellaceae; Kangiella.
OX   NCBI_TaxID=523791 {ECO:0000313|EMBL:ACV26519.1, ECO:0000313|Proteomes:UP000001231};
RN   [1] {ECO:0000313|EMBL:ACV26519.1, ECO:0000313|Proteomes:UP000001231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16069 / KCTC 12182 / SW-125
RC   {ECO:0000313|Proteomes:UP000001231};
RX   PubMed=21304661; DOI=10.4056/sigs.36635;
RA   Han C., Sikorski J., Lapidus A., Nolan M., Glavina Del Rio T., Tice H.,
RA   Cheng J.F., Lucas S., Chen F., Copeland A., Ivanova N., Mavromatis K.,
RA   Ovchinnikova G., Pati A., Bruce D., Goodwin L., Pitluck S., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA   Saunders E., Brettin T., Goker M., Tindall B.J., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT   "Complete genome sequence of Kangiella koreensis type strain (SW-125).";
RL   Stand. Genomic Sci. 1:226-233(2009).
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         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|ARBA:ARBA00046318, ECO:0000256|PIRNR:PIRNR009407}.
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DR   EMBL; CP001707; ACV26519.1; -; Genomic_DNA.
DR   RefSeq; WP_012801033.1; NC_013166.1.
DR   AlphaFoldDB; C7RB77; -.
DR   STRING; 523791.Kkor_1100; -.
DR   KEGG; kko:Kkor_1100; -.
DR   eggNOG; COG2838; Bacteria.
DR   HOGENOM; CLU_025308_1_0_6; -.
DR   InParanoid; C7RB77; -.
DR   OrthoDB; 9807643at2; -.
DR   Proteomes; UP000001231; Chromosome.
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; 1.
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   3: Inferred from homology;
KW   Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435,
KW   ECO:0000256|PIRNR:PIRNR009407};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR009407-3};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR009407-3};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR009407};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR009407};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001231};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW   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="D-threo-isocitrate"
FT                   /ligand_id="ChEBI:CHEBI:15562"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         350
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         547
FT                   /ligand="D-threo-isocitrate"
FT                   /ligand_id="ChEBI:CHEBI:15562"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         548
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         552
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         584..585
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         589
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         600..602
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         649
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   SITE            255
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT   SITE            420
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ   SEQUENCE   740 AA;  81223 MW;  1D5F7D181DB841EA CRC64;
     MTSSKIIYTK TDEAPALATY SLLPIVEAFA KAAGIEVETS DISLAGRVIA SFPEYLKEEQ
     RIPDALAELG ELVKKPEANI IKLPNISASI PQLKATIKEL QDKGYALPDY PDNASSDEEK
     DIRNRYDKIK GSAVNPVLRE GNSDRRAPNA VKNYAKKNPH SMGEWSKDSK SHVASMQSGD
     FFSNEKSITV DGNNDVKIEF VGNDGSKQVL KESTPLLAGE VIDATVLNKN ALVKFLEEQV
     EDAKKQDVLF SLHMKATMMK VSDPIIFGHG VKVFFKDVFE KHADALAQVG ANPNNGFGNV
     LSAIESLPAE KRDEIKADIE AVYAKNPELA MVNSDKGITN LHVPSDVIID ASMPAMIRTS
     GMMWGPDGQP KDTKAVIPDS SYSGVYSATI DFCREHGAFD PRTMGTVPNV GLMAQKAEEY
     GSHDKTFEMT GNGHVRVTDK DGNVVLEHAV EEGDIWRMCQ VKDAPIRDWV KLAVTRSRLS
     GMPAVFWLDK NRAHDAQLIQ KVETYLKDHD TSGLEIHIMS PVDATKFTLQ RMKDGKDTIS
     VTGNVLRDYL TDLFPILELG TSAKMLSIVP LMNGGGLFET GAGGSAPKHV QQFMEENHLR
     WDSLGEFLAL AVSFEHMAQT TNNKKAQVLA DTLDRATGKF LDNGKSPSRK VNELDNRGSH
     FYLAMYWAQE LASQTDDAEL KGLFAKVSEA LTSNEAKIVD ELNAVQGQAM DIGGYYKPDD
     NLGFKAMRPS TTLNTALELI
//