ID   Q0PAY5_CAMJE            Unreviewed;       734 AA.
AC   Q0PAY5;
DT   19-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   19-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 102.
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:CAL34677.1};
GN   OrderedLocusNames=Cj0531 {ECO:0000313|EMBL:CAL34677.1};
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 /
OS   NCTC 11168).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222 {ECO:0000313|EMBL:CAL34677.1, ECO:0000313|Proteomes:UP000000799};
RN   [1] {ECO:0000313|EMBL:CAL34677.1, ECO:0000313|Proteomes:UP000000799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168 {ECO:0000313|Proteomes:UP000000799};
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K., Ketley J.M., Churcher C., Basham D.,
RA   Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K.,
RA   Karlyshev A., Moule S., Pallen M.J., Penn C.W., Quail M., Rajandream M.A.,
RA   Rutherford K.M., VanVliet A., Whitehead S., Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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; AL111168; CAL34677.1; -; Genomic_DNA.
DR   PIR; C81399; C81399.
DR   RefSeq; WP_002858520.1; NZ_SZUC01000002.1.
DR   RefSeq; YP_002343962.1; NC_002163.1.
DR   AlphaFoldDB; Q0PAY5; -.
DR   IntAct; Q0PAY5; 7.
DR   STRING; 192222.Cj0531; -.
DR   PaxDb; 192222-Cj0531; -.
DR   EnsemblBacteria; CAL34677; CAL34677; Cj0531.
DR   GeneID; 904859; -.
DR   KEGG; cje:Cj0531; -.
DR   PATRIC; fig|192222.6.peg.523; -.
DR   eggNOG; COG2838; Bacteria.
DR   HOGENOM; CLU_025308_1_0_7; -.
DR   OrthoDB; 9807643at2; -.
DR   Proteomes; UP000000799; 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};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR009407,
KW   ECO:0000313|EMBL:CAL34677.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000799};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT   BINDING         129..136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         345
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         538
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         539
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         543
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   SITE            252
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT   SITE            415
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ   SEQUENCE   734 AA;  82331 MW;  39E62BC90977B41B CRC64;
     MQITYTLTDE SPALATYSFL PIVKAFLSRA HIGVKTSDIS LSGRILATFS EYLKEEQRCE
     DALELLGELV KRSDANLIKT PNISASIPQL KAAIKELQDK GYMLPNYPDE PKNDEELQIK
     TKYQKVLGSA VNPVLRQGNS DRRSTKAVKD YAKNNPYRVV EFNPNSKTRV SYMKEGDFFS
     NEKAVLIDQD CVANIEFTSV DGKKEILKEG LKLEKNEILD ATFMDVQKLQ EFYAKEIKAS
     KDDDVLFSLH LKATMMKVSD PILFGYAVKV FFKELFIEFQ DEFEKLGINP NNGLSELLSK
     IENSSKKDEI LKKYSEILAK SADISMVNSD KGITNLHVPS DVIVDASMPA MLKNGARLWD
     KEGKEKDTNA VIPDQTYATI YEAVIEDLHK NGTLNPSKLG SVSNVGLMAK KAQEYGSHDK
     TFVAKEEGTF KIVSNGKVLL EHKVRKGDIY RANQAKFDAV LNWIDLGIER SELSGAEAIF
     WLDSKRASNK IMITLVQNRL KEKGKNVAIL TPKEACLRSL ELIREGKDVI SITGNVLRDY
     LTDLFPILEL GTSAKMLSVV PMLNGGAMFE TGAGGSAPKQ VEQLVEENHL RWDSLGEFLA
     LQASLEFYAN KCGNHKAKVL AECLDEAIGE WLENNKAPSR KVKEDDNRTS HFYLAMYFAN
     HLARQASDME LQSFFKDIAL ELSSNEEKIR AEFNDAQGVK VDLGGYYKFD DEKANKIMRP
     SATFNAILEK IGQR
//