ID   ACEK2_PSET1             Reviewed;         571 AA.
AC   Q3IHD9;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Isocitrate dehydrogenase kinase/phosphatase 2 {ECO:0000255|HAMAP-Rule:MF_00747};
DE            Short=IDH kinase/phosphatase 2 {ECO:0000255|HAMAP-Rule:MF_00747};
DE            Short=IDHK/P 2 {ECO:0000255|HAMAP-Rule:MF_00747};
DE            EC=2.7.11.5 {ECO:0000255|HAMAP-Rule:MF_00747};
DE            EC=3.1.3.- {ECO:0000255|HAMAP-Rule:MF_00747};
GN   Name=aceK2 {ECO:0000255|HAMAP-Rule:MF_00747}; OrderedLocusNames=PSHAa1821;
OS   Pseudoalteromonas translucida (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C.,
RA   Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT   Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Bifunctional enzyme which can phosphorylate or
CC       dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine
CC       residue. This is a regulatory mechanism which enables bacteria to
CC       bypass the Krebs cycle via the glyoxylate shunt in response to the
CC       source of carbon. When bacteria are grown on glucose, IDH is fully
CC       active and unphosphorylated, but when grown on acetate or ethanol, the
CC       activity of IDH declines drastically concomitant with its
CC       phosphorylation. {ECO:0000255|HAMAP-Rule:MF_00747}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[isocitrate dehydrogenase] = ADP + H(+) + O-
CC         phospho-L-seryl-[isocitrate dehydrogenase]; Xref=Rhea:RHEA:43540,
CC         Rhea:RHEA-COMP:10605, Rhea:RHEA-COMP:10606, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
CC         ChEBI:CHEBI:456216; EC=2.7.11.5; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00747};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00747}.
CC   -!- SIMILARITY: Belongs to the AceK family. {ECO:0000255|HAMAP-
CC       Rule:MF_00747}.
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DR   EMBL; CR954246; CAI86893.1; -; Genomic_DNA.
DR   RefSeq; WP_011328496.1; NC_007481.1.
DR   AlphaFoldDB; Q3IHD9; -.
DR   SMR; Q3IHD9; -.
DR   STRING; 326442.PSHAa1821; -.
DR   EnsemblBacteria; CAI86893; CAI86893; PSHAa1821.
DR   KEGG; pha:PSHAa1821; -.
DR   PATRIC; fig|326442.8.peg.1769; -.
DR   eggNOG; COG4579; Bacteria.
DR   HOGENOM; CLU_033804_1_1_6; -.
DR   OMA; EPWYSVG; -.
DR   OrthoDB; 245269at2; -.
DR   BioCyc; PHAL326442:PSHA_RS08930-MON; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008772; F:[isocitrate dehydrogenase (NADP+)] kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00747; AceK; 1.
DR   InterPro; IPR010452; Isocitrate_DH_AceK.
DR   PANTHER; PTHR39559; PTHR39559; 1.
DR   Pfam; PF06315; AceK; 1.
DR   PIRSF; PIRSF000719; AceK; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Glyoxylate bypass; Hydrolase; Kinase;
KW   Nucleotide-binding; Protein phosphatase; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase; Tricarboxylic acid cycle.
FT   CHAIN           1..571
FT                   /note="Isocitrate dehydrogenase kinase/phosphatase 2"
FT                   /id="PRO_0000288294"
FT   ACT_SITE        369
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT   BINDING         313..319
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT   BINDING         334
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
SQ   SEQUENCE   571 AA;  66954 MW;  73397FF3DE21EDBF CRC64;
     MQPRHIAELI LTGFKKHYLL FQKTTAKAPL AFAKRDWQAI NDISRLRISH YDDRVNETTA
     TLRQQQTEQL DEQLWLEVKK LYQHFLCFHP QAELAETFYN SVFCRLYHRR YFHNDFIFVE
     ATLKDAPAVP VEAEYRSYFP VVDGLKPTIK QIINHFDFKA PFVNLERDIR LLVKAFYKQA
     PDTHHKAWQM RFDILHTPFY RNKAAYIVGR VVSQSGVQPF IIAVLHHEDK GLYLDALLTK
     SSQMRVIFGF ARAYFMVETH APCALVRFLN QLMPNKTIAE LYNAIGFHKQ GKTEFYREFL
     NHLTHSNDEF TIAPGTPGMV MMVFTLPSFG YVFKVIKDKF GESKPFGRDT VLKRYQLVKK
     HDRVGRMADT IEYSNVVFPL ARFDSNLLQQ LHQTIGSSMV IEGDWLIIKH LYIERRMTPL
     NLFLENADDA SAADAIEEYG QALKEMIAVN IFPGDMLLKN FGVSKHKRII FYDYDEVQYL
     TDMNFRALPK AKTYDDYLMD EQSYSVAPQD VFPEQLCTFV MPNPIYKQFL MSTHPELIDV
     NFWKQAQQNI KNGQVSHIYP YPTAQRFIHH W