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Database: UniProt
Entry: U4KFX5_9VIBR
LinkDB: U4KFX5_9VIBR
Original site: U4KFX5_9VIBR 
ID   U4KFX5_9VIBR            Unreviewed;       742 AA.
AC   U4KFX5;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
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   Name=icd {ECO:0000313|EMBL:CCO58213.1};
GN   ORFNames=VIBNI_A2132 {ECO:0000313|EMBL:CCO58213.1};
OS   Vibrio nigripulchritudo.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=28173 {ECO:0000313|EMBL:CCO58213.1, ECO:0000313|Proteomes:UP000016895};
RN   [1] {ECO:0000313|EMBL:CCO58213.1, ECO:0000313|Proteomes:UP000016895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SnF1 {ECO:0000313|Proteomes:UP000016895};
RX   PubMed=23739050; DOI=10.1038/ismej.2013.90;
RA   Goudenege D., Labreuche Y., Krin E., Ansquer D., Mangenot S., Calteau A.,
RA   Medigue C., Mazel D., Polz M.F., Le Roux F.;
RT   "Comparative genomics of pathogenic lineages of Vibrio nigripulchritudo
RT   identifies virulence-associated traits.";
RL   ISME J. 7:1985-1996(2013).
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; FO203526; CCO58213.1; -; Genomic_DNA.
DR   RefSeq; WP_022551023.1; NC_022528.1.
DR   AlphaFoldDB; U4KFX5; -.
DR   STRING; 28173.VIBNI_A2132; -.
DR   KEGG; vni:VIBNI_A2132; -.
DR   PATRIC; fig|1260221.3.peg.2024; -.
DR   eggNOG; COG2838; Bacteria.
DR   OrthoDB; 9807643at2; -.
DR   Proteomes; UP000016895; Chromosome 1.
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:CCO58213.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016895};
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   742 AA;  80639 MW;  6FB5466A8531D9EA CRC64;
     MPTTKPTIIY TITDEAPALA TYSLLPIIRA FTSSSDINVE TRDISLAGRI IANFPDYLTE
     EQRIGDALSE LGELAKTPEA NIIKLPNISA SVPQLQAAIK ELQAKGYALP NYPEEPKTDE
     EAKVKAVYDK IKGSAVNPVL REGNSDRRAP ASVKNYAKKN PHSMGAWSAE SKSHVASMSG
     NDFFGSEKSV TINGATNVRI EFVGTDGEVK VLKSEFALQD QEIIDASVMN KAALVSFFEK
     EIEEAKEQDV LLSLHMKATM MKVSDPVIFG HAVSVYYKEV FDKYQDVFEQ LGVDVNNGIG
     DVYAKITSLP EAQQEEIKAA LQAVYETRPA LAMVDSDRGI TNLHVPSDVI VDASMPAMLR
     SSGQMWGPDG KLKDTKAMIP DRSYASVYQA VIEFCKENGA FDPTTMGSVP NVGLMAQKAE
     EYGSHDKTFI QQAAGKVRVV DSAGTVLIEQ DVEEGDIFRM CQVKDAPIQD WVKLAVNRAR
     ATGAPAVFWL DESRAHDAEL IKKVNAYLPE HDTSGLEIKI LSPLEATKFS LVRIKDGLDT
     ISVTGNVLRD YLTDLFPILE LGTSAKMLSI VPLMNGGGLF ETGAGGSAPK HVQQVEKENH
     LRWDSLGEFL ALAASLEHLS NVTGNKKAQV LADALDKATG EFLDNNKSPS RKVGELDNRG
     SHFYLASYWA KALAEQSDDA ELSTQFGPIA KQMAENEDAI VKQLNDAQGV VGELGGYYAP
     EDAKAAPLMR PSDLLNGIVD AV
//
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