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Database: UniProt/TrEMBL
Entry: D1BGD8_SANKS
LinkDB: D1BGD8_SANKS
Original site: D1BGD8_SANKS 
ID   D1BGD8_SANKS            Unreviewed;       736 AA.
AC   D1BGD8;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   24-JAN-2024, entry version 71.
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=Sked_37720 {ECO:0000313|EMBL:ACZ23655.1};
OS   Sanguibacter keddieii (strain ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Sanguibacteraceae;
OC   Sanguibacter.
OX   NCBI_TaxID=446469 {ECO:0000313|EMBL:ACZ23655.1, ECO:0000313|Proteomes:UP000000322};
RN   [1] {ECO:0000313|EMBL:ACZ23655.1, ECO:0000313|Proteomes:UP000000322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74
RC   {ECO:0000313|Proteomes:UP000000322};
RX   PubMed=21304646;
RA   Ivanova N., Sikorski J., Sims D., Brettin T., Detter J.C., Han C.,
RA   Lapidus A., Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S.,
RA   Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Pati A.,
RA   Mavromatis K., Chen A., Palaniappan K., D'haeseleer P., Chain P.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Goker M., Pukall R.,
RA   Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Sanguibacter keddieii type strain (ST-74).";
RL   Stand. Genomic Sci. 1:110-118(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|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}.
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DR   EMBL; CP001819; ACZ23655.1; -; Genomic_DNA.
DR   RefSeq; WP_012868723.1; NC_013521.1.
DR   AlphaFoldDB; D1BGD8; -.
DR   STRING; 446469.Sked_37720; -.
DR   KEGG; ske:Sked_37720; -.
DR   eggNOG; COG2838; Bacteria.
DR   HOGENOM; CLU_025308_1_0_11; -.
DR   OMA; FRMCQTK; -.
DR   OrthoDB; 9807643at2; -.
DR   Proteomes; UP000000322; 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:ACZ23655.1};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT   BINDING         80..85
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         130..137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         133
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         346
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         543
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         544
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         548
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         580..581
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         585
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         596..598
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         645
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   SITE            253
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT   SITE            416
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ   SEQUENCE   736 AA;  78819 MW;  DCD622819023F1D7 CRC64;
     MSKIIYTYTD EAPMLATHSF LPVVSAFAGT AGVELETRDI SLAGRIIAAF PERLTDAQRI
     GDALAELGEL ATTPEANIIK LPNVSASLPQ LKAAIAELQA QGYDLPDHPD APATDADEDV
     RARYDKIKGS AVNPVLREGN SDRRAPLSVK EYVRKNPHRM GAWTADSKTN VATMGHDDFF
     SNEKSVVLDA DDVLRIEHVS ASGDVTVLHP GVKVLAGEVV DASFLDVAEL HTFLADAIAR
     AKAEDVLFSV HLKATMMKVS DPIIFGHVVR AFFPAVFEQY GADLEAAGLS PNNGLGGILD
     GLAALPNGDE IRAAFDKGLA DGPRLAMVNS DKGITNLHVP SDVIVDASMP AMIRTSGHMW
     GPDGSEQDTI AVIPDSSYAG IYQAVIDDCR ANGAYDPTTM GTVPNVGLMA QKAEEYGSHD
     KTFEVAEAGT VRVVNQAGEA LLEHEVRAGD IWRACQTKDV AIRDWVKLAV NRARATGTLT
     VFWLDEKRAH DANLIKKVEA YLPEHDTTGL DIRVLAPAEA TTLSVERIRR GEDTISVTGN
     VLRDYNTDLF PILELGTSAK MLSIVPLLNG GGLFETGAGG SAPKHVQQLV EENYLRWDSL
     GEFLALAASF EHFADVNSNE KARVLGATLD RATGTFLLEN KSPGRKLGTI DNRGSHFFLA
     LFWAEELAQQ TDDADLAAAF GPLAASLRAD EQTIVDELVA VQGSPAEIGG YYKVDAAKTD
     AVMRPSATFT AALAAL
//
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