ACEK_XANCP
ID ACEK_XANCP Reviewed; 579 AA.
AC Q8P4D0;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Isocitrate dehydrogenase kinase/phosphatase {ECO:0000255|HAMAP-Rule:MF_00747};
DE Short=IDH kinase/phosphatase {ECO:0000255|HAMAP-Rule:MF_00747};
DE Short=IDHK/P {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=aceK {ECO:0000255|HAMAP-Rule:MF_00747}; OrderedLocusNames=XCC3780;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
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}.
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; AE008922; AAM43480.1; -; Genomic_DNA.
DR RefSeq; NP_639125.1; NC_003902.1.
DR RefSeq; WP_011038861.1; NC_003902.1.
DR AlphaFoldDB; Q8P4D0; -.
DR SMR; Q8P4D0; -.
DR STRING; 340.xcc-b100_3962; -.
DR EnsemblBacteria; AAM43480; AAM43480; XCC3780.
DR KEGG; xcc:XCC3780; -.
DR PATRIC; fig|190485.4.peg.4046; -.
DR eggNOG; COG4579; Bacteria.
DR HOGENOM; CLU_033804_1_1_6; -.
DR OMA; EPWYSVG; -.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008772; F:[isocitrate dehydrogenase (NADP+)] kinase activity; IBA:GO_Central.
DR GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
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:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0050790; P:regulation of catalytic activity; IBA:GO_Central.
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..579
FT /note="Isocitrate dehydrogenase kinase/phosphatase"
FT /id="PRO_0000057911"
FT ACT_SITE 380
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT BINDING 324..330
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT BINDING 345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
SQ SEQUENCE 579 AA; 66976 MW; 2A8D77113DFC8FD2 CRC64;
MNQQPLPPQS ERRALAIGRA VYEAFQDYHA QFSQITARAR QRFETRDWSG AREDAVARIA
LYDHYISECM LRLRAVLLGQ AHDRALWMRA RTHYAELLTG LIDQELYKTF YNTLTRRYFR
TQGVDAQIEF IALDIEPTDA ITVPVARHTY AVSPGRLTEM LVRVLGDYPF EVPYAHRTRC
AAAIAVRLLD DLAHWGEHPV RSVELLETVF YRERRAYLVG RLFGEHRFSP CVIALVNDDA
GLRAEAVLTR RSDVAQLFSN SRSYFQADLT TVGDAVVFLR SLLTHKPIDE LYTMLGRAKQ
GKTERYRTFF RHFQAHPAEQ LVHADGTPGM VMVVFTLPSY PLVFKLIRDR FAYPKTMSRA
QVEGKYELVF QLDRIGRLLD AQPYRFLRFP KARFSPALLQ DLQSSCAMSL SEDGDDVLIA
LCYVQRRLRP LNLYLREQLP AAAHAAALDY GQAIKDMARN NIFPGDMLLK NFGITRHQRA
VFYDYDELCL ITECTFRDWP TPTSYEEQMA AEPWFHVGPR DVFPERFALF MGLPSSQLEA
VKHMHPELFD PQWWRDLQAR LREDDYPDTP PYADAQKLA
