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 24-JUL-2024, entry version 96.
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; Pseudomonadota; 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 AlphaFoldDB; Q3IHD9; -.
DR SMR; Q3IHD9; -.
DR STRING; 326442.PSHAa1821; -.
DR KEGG; pha:PSHAa1821; -.
DR PATRIC; fig|326442.8.peg.1769; -.
DR eggNOG; COG4579; Bacteria.
DR HOGENOM; CLU_033804_1_1_6; -.
DR BioCyc; PHAL326442:PSHA_RS08930-MONOMER; -.
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:0016208; F:AMP binding; IEA:TreeGrafter.
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:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00747; AceK; 1.
DR InterPro; IPR046855; AceK_kinase.
DR InterPro; IPR046854; AceK_regulatory.
DR InterPro; IPR010452; Isocitrate_DH_AceK.
DR PANTHER; PTHR39559; -; 1.
DR PANTHER; PTHR39559:SF1; ISOCITRATE DEHYDROGENASE KINASE_PHOSPHATASE; 1.
DR Pfam; PF06315; AceK_kinase; 1.
DR Pfam; PF20423; AceK_regulatory; 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
//
