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Database: UniProt
Entry: A0A0B8NP36_9VIBR
LinkDB: A0A0B8NP36_9VIBR
Original site: A0A0B8NP36_9VIBR 
ID   A0A0B8NP36_9VIBR        Unreviewed;       743 AA.
AC   A0A0B8NP36;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
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   ORFNames=JCM19231_1012 {ECO:0000313|EMBL:GAM56355.1};
OS   Vibrio ishigakensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1481914 {ECO:0000313|EMBL:GAM56355.1, ECO:0000313|Proteomes:UP000031671};
RN   [1] {ECO:0000313|EMBL:GAM56355.1, ECO:0000313|Proteomes:UP000031671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 19231 {ECO:0000313|Proteomes:UP000031671};
RA   Sawabe T., Meirelles P., Feng G., Sayaka M., Hattori M., Ohkuma M.;
RT   "Vibrio sp. C1 JCM 19231 whole genome shotgun sequence.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAM56355.1, ECO:0000313|Proteomes:UP000031671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 19231 {ECO:0000313|Proteomes:UP000031671};
RG   NBRP consortium;
RA   Sawabe T., Meirelles P., Feng G., Sayaka M., Hattori M., Ohkuma M.;
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAM56355.1}.
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DR   EMBL; BBRZ01000028; GAM56355.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B8NP36; -.
DR   Proteomes; UP000031671; Unassembled WGS sequence.
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   ECO:0000313|EMBL:GAM56355.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031671};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
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         352
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         549
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         550
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         554
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         586..587
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         591
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         602..604
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         651
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   SITE            257
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT   SITE            422
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ   SEQUENCE   743 AA;  80713 MW;  5829D15622D2F001 CRC64;
     MSDQKPTIIY TITDEAPALA TYSLLPMIQS FTASSGIAVD TRDISLAGRI IANFAEYLKP
     EQRIGDALSE LGELAKTPEA NIIKLPNISA SIPQLKAAIA ELQAKGYDLP NYPEEPSSDE
     EKAIQSIYDK IKGSAVNPVL REGNSDRRAP ASVKNYAKKN PHSMGKWESN SQSHVSSMQD
     SDFFGSEKST TISGETSVRI ELRGADGSVE TLKSEFPLQD KEIIDTAVMN KKALVAFFEQ
     QIEDAKQNDV LLSLHMKATM MKVSDPVIFG HAVKVYYKDV FEKHGEVFEQ LGVDVNNGIG
     DVYAKIESLP AEQKAKIIAD LEAVYETRPA LAMVDSDRGI TNLHVPSDVI VDASMPAMIR
     SSGQMWGPDG KQKDTKAMIP DRSYAGVYQA VIEFCKEHGA FDPTTMGSVP NVGLMAQKAE
     EYGSHDKTFI LSKAGTVAVV DASGAVLLEQ SVEEGDIFRM CQVKDAPIQD WVKLAVNRSR
     LSDTPAVFWL DANRAHDAQL IKKVEEYLPQ HDTDGLDIRI LSPVDATLFS VERIAKGQDT
     ISVTGNVLRD YLTDLFPILE LGTSAKMLSI VPLMNGGGLF ETGAGGSAPK HVQQVEKENH
     LRWDSLGEFL ALAASLEHLS EVTGNAKAKV LASTLDAATG RFLDENKSPS RRVNELDNRG
     SHYYLASFWA EALSLQNKDA ELAAQFEPVA KALRDSEATI VAELNGAQGV AGELGGYYAP
     QDELASKLMR PSATLNAIID ALA
//
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