ID A0A090U1G1_9VIBR Unreviewed; 740 AA.
AC A0A090U1G1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=JCM19240_3818 {ECO:0000313|EMBL:GAL36852.1};
OS Vibrio maritimus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=990268 {ECO:0000313|EMBL:GAL36852.1, ECO:0000313|Proteomes:UP000029224};
RN [1] {ECO:0000313|EMBL:GAL36852.1, ECO:0000313|Proteomes:UP000029224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19240 {ECO:0000313|EMBL:GAL36852.1,
RC ECO:0000313|Proteomes:UP000029224};
RA Sawabe T., Meirelles P., Nakanishi M., Sayaka M., Hattori M., Ohkuma M.;
RT "Vibrio maritimus JCM 19240. (C210) whole genome shotgun sequence.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAL36852.1, ECO:0000313|Proteomes:UP000029224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19240 {ECO:0000313|EMBL:GAL36852.1,
RC ECO:0000313|Proteomes:UP000029224};
RG NBRP consortium;
RA Sawabe T., Meirelles P., Nakanishi M., Sayaka M., Hattori M., Ohkuma M.;
RL Submitted (SEP-2014) 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:GAL36852.1}.
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DR EMBL; BBMT01000013; GAL36852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090U1G1; -.
DR OrthoDB; 9807643at2; -.
DR Proteomes; UP000029224; 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; 2.
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:GAL36852.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029224};
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 740 AA; 80038 MW; 29B9A4BAD0438B3A CRC64;
MPTEKPTIIY TITDEAPALA TYSLLPIIQS FTASSGIDVD TRDISLAGRI IANFPDYLKE
EQRIGDALAE LGELAKTPEA NIIKLPNISA SIPQLQAAIK ELQANGYALP DYPEEPANAE
QEAIKATYDK IKGSAVNPVL REGNSDRRAP LSVKNYAKKN PHSMGAWSKD SKSHVASMSG
NDFFGSEKSV TTESATDVQI RFTSASGETK VLKDKVALQA GEIIDASVMN KNALVAFFEE
QIEEAKQQDV LLSLHMKATM MKVSDPVIFG HAVKVYYKAV FDKYAALFEE LGVDVNNGIG
DVYAKIASLP AAQKAEIEAD LAAVYETQPP LAMVDSDRGI TNLHVPSDII VDASMPAMLR
SSGQMWGPDG KQKDTKAMIP DRSYASIYQA VIDFCKQHGA FDPTTMGSVP NVGLMAQKAE
EYGSHDKTFI LDAAGTVSVV DAEGNVLIEQ QVEEGDIFRM CQVKDAPIQD WVKLAVTRAR
ASSTPAVFWL DENRAHDAEL IKKVNQYLPE HDTAGLEIHI KSPLEATLFS LERIKEGLDT
ISVTGNVLRD YLTDLFPILE LGTSAKMLSI VPLMNGGGLF ETGAGGSAPK HVQQVQKENH
LRWDSLGEFL ALAASLEHLA VVSGKEKANV LAKALDAATG KFLDNNKSPS RKVGELDNRG
SHYYLALYWA QALAVQTEDA SLAEEFAPIA EQLASNESII VSELNNAQGV AGDLGGYYQP
SDAKASTLMR PSATLNSIID
//
