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 / NCTC
OS 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//
