ID C5NMM8_9PSED Unreviewed; 741 AA.
AC C5NMM8; S6HS60;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 67.
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-M {ECO:0000313|EMBL:BAH80317.1};
OS Pseudomonas psychrophila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=122355 {ECO:0000313|EMBL:BAH80317.1};
RN [1] {ECO:0000313|EMBL:BAH80317.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20549192; DOI=10.1007/s00203-010-0595-3;
RA Matsuo S., Shirai H., Takada Y.;
RT "Isocitrate dehydrogenase isozymes from a psychrotrophic bacterium,
RT Pseudomonas psychrophila.";
RL Arch. Microbiol. 192:639-650(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; AB425997; BAH80317.1; -; Genomic_DNA.
DR RefSeq; WP_019828505.1; NZ_VZPR01000009.1.
DR AlphaFoldDB; C5NMM8; -.
DR SMR; C5NMM8; -.
DR PATRIC; fig|122355.7.peg.1103; -.
DR eggNOG; COG2838; Bacteria.
DR OrthoDB; 9807643at2; -.
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 Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT BINDING 82..87
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 132..139
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 135
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 145
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; 80633 MW; 4A544EBAB254AAC1 CRC64;
MPNRSKIIYT FTDEAPALAT YSLLPIIEAF TAPADIAVET RDISLAGRIL ASFPEQLGAK
AVADHLAELG ALAVTPEANI IKLPNISASV PQLQAAIKEL QAQGFDIPDY PETVTTDADK
EVKARYSKVM GSAVNPVLRE GNSDRRAPLS VKNYARKHPH KMGAWAADSK SHVAHMSEGD
FYASEKAALI EAPGSVKIEL IAQDGTTTVL KEKTAVQAGE IIDCSVMSKK ALRQFVAAEI
EDAKKQGVLF SVHLKATMMK VSDPIMFGQI VAEFYKDALE KHADILKEIG FNLNNGIGDL
YARIKALPAE KQAEIEADIQ AVYANRPALA MVNSDKGITN LHVPSDVIVD ASMPAMIRDS
GKMWNTEGQL QDTKAVIPDR CYATIYQATI EDCQKHGAFD PTTMGSVPNV GLMAQKAEEY
GSHDKTFQIK TPGVVRVTDS NGNVLMEQNV EEGDIWRMCQ AKDAPIRDWV KLAVNRARAS
NTPAVFWLDP KRSHDAEMIK KVETYLKDHD TSGLDIRIMA PVDAMKFTLE RTRAGLDTIS
VTGNVLRDYL TDLFPIMELG TSAKMLSIVP LMNGGGLFET GAGGSAPKHV QQLLEENFLR
WDSLGEFLAL AASLEHLGTT YNNPKALVLA KTLDQATGQF LDNNKSPSRK VGNIDNRGSH
FYLALYWAQA LAAQTEDKEL QAQFAPVAKA MAENEAKIVA ELNAVQGKPV DIGGYYHADA
DKLSKVMRPS ATLNAIIASL V
//
