ID A6V4G2_PSEA7 Unreviewed; 741 AA.
AC A6V4G2;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, 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=PSPA7_2583 {ECO:0000313|EMBL:ABR86332.1};
OS Pseudomonas aeruginosa (strain PA7).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=381754 {ECO:0000313|EMBL:ABR86332.1, ECO:0000313|Proteomes:UP000001582};
RN [1] {ECO:0000313|EMBL:ABR86332.1, ECO:0000313|Proteomes:UP000001582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA7 {ECO:0000313|EMBL:ABR86332.1,
RC ECO:0000313|Proteomes:UP000001582};
RA Dodson R.J., Harkins D., Paulsen I.T.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABR86332.1, ECO:0000313|Proteomes:UP000001582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA7 {ECO:0000313|EMBL:ABR86332.1,
RC ECO:0000313|Proteomes:UP000001582};
RX PubMed=20107499; DOI=10.1371/journal.pone.0008842;
RA Roy P.H., Tetu S.G., Larouche A., Elbourne L., Tremblay S., Ren Q.,
RA Dodson R., Harkins D., Shay R., Watkins K., Mahamoud Y., Paulsen I.T.;
RT "Complete genome sequence of the multiresistant taxonomic outlier
RT Pseudomonas aeruginosa PA7.";
RL PLoS ONE 5:E8842-E8842(2010).
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; CP000744; ABR86332.1; -; Genomic_DNA.
DR RefSeq; WP_012075453.1; NC_009656.1.
DR AlphaFoldDB; A6V4G2; -.
DR GeneID; 77220839; -.
DR KEGG; pap:PSPA7_2583; -.
DR HOGENOM; CLU_025308_1_0_6; -.
DR Proteomes; UP000001582; 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:ABR86332.1};
KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT BINDING 83..88
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 133..140
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 136
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 350
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 547
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 548
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 552
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
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 741 AA; 81664 MW; AA62275196699886 CRC64;
MSIRSKITYT FTDEAPALAT YSLLPIVKAF AASAGIDVET SDISLAGRIL ANFADRLEAD
QRIEDDLARL AVLATSPDAN IIKLPNISAS VPQLKGAIAE LQALGYKVPD FPEDPQTDEE
KEVRARYAKI LGSAVNPVLR EGNSDRRAPA AVKAYARKHP HSMGKWSMAS RSHADYMRGG
DFFSSEQSIT MAKAGDVRIE FVGKDGKVEV KKQLSLQEGE VLDSMFMSCG KLRDFFEKTL
QDCKETGVMW SLHVKATMMK ISHPIVFGHA VSVYYKDVFD KWGQLFEELG VNPNNGISSV
YDKIKSLPAS QQEEILHDIH EVYSHRPEMA MVDSVKGITN LHIPSDVIVD ASMPAMIRNS
GQMWGKDGKQ KDTKAVMPES TYARIYQEMI NFCKTNGAFD PTTMGSVPNV GLMAQKAEEY
GSHDKTFEMT ADGTMRVVLA DGTVLMQHEV ETGDIWRACQ TKDAPIRDWV KLAVTRARQS
DTPAIFWLDP ERAHDRELRK KVELYLKDHD LTGLDISIMG YNEAIRVSME RLIRGKDTIS
VTGNVLRDYL TDLFPIMELG TSAKMLSIVP LMAGGGMYET GAGGSAPKHV QQLVEENYLR
WDSLGEFLAL AVSLEETGIK TGNAKAKLLG KALDEATGKL LDNNKSPSRK VGDIDNRGSH
FYLAMYWAQA LAAQDEDAEL KAHFAPLAKA LTEQEATIVA ELNAVQGKPA EIGGYYRSNP
ELTSKVMRPS ATFNAAIDSL A
//
