ACEK1_PSET1
ID ACEK1_PSET1 Reviewed; 592 AA.
AC Q3IKY9;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Isocitrate dehydrogenase kinase/phosphatase 1 {ECO:0000255|HAMAP-Rule:MF_00747};
DE Short=IDH kinase/phosphatase 1 {ECO:0000255|HAMAP-Rule:MF_00747};
DE Short=IDHK/P 1 {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=aceK1 {ECO:0000255|HAMAP-Rule:MF_00747}; OrderedLocusNames=PSHAa1307;
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; CAI86382.1; -; Genomic_DNA.
DR RefSeq; WP_011327988.1; NC_007481.1.
DR AlphaFoldDB; Q3IKY9; -.
DR SMR; Q3IKY9; -.
DR STRING; 326442.PSHAa1307; -.
DR PRIDE; Q3IKY9; -.
DR EnsemblBacteria; CAI86382; CAI86382; PSHAa1307.
DR KEGG; pha:PSHAa1307; -.
DR PATRIC; fig|326442.8.peg.1263; -.
DR eggNOG; COG4579; Bacteria.
DR HOGENOM; CLU_033804_1_1_6; -.
DR OMA; THEFRYL; -.
DR OrthoDB; 245269at2; -.
DR BioCyc; PHAL326442:PSHA_RS06435-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..592
FT /note="Isocitrate dehydrogenase kinase/phosphatase 1"
FT /id="PRO_0000288293"
FT ACT_SITE 393
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT BINDING 337..343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT BINDING 358
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
SQ SEQUENCE 592 AA; 68071 MW; E076B5CAA8D9BFDA CRC64;
MPDTITNKLQ NSTVQDVIAT KLARAVFAGF EAMFATFLNI TLGAQSRFEQ RQYHEVQSAM
RERLQVYERQ VKSVSEAVKV IAYAELSCPQ TWQLAKNIYG NMVKNHENEP IAHTFFNSTF
GAIWDDKKIR TVHLFVLKAK YRTQPRPYDS LVKRISLQHG FNSAIKTLIT NQVFRVPFSN
LNQDVATLQA TLTQGAKQQC RQVYELINLN DGYIEYAYSH FYRNKACYLI GRCIAKNGDN
MPFAIAILNT PKGLKIDAVM MGADQLSLLF GFARTYFMVD TDQPARYVDY LSVLMPHKQR
FELFNAIGFI KHAKTEFYRY KVDTTKNSPA SFKYVAAPGT PGMVMLVFTI AGSDHVYKVI
KDKFSAPKTA TKAQVKEKYN FVKQADRVGR LVDTHEFRYL AFDLSRFSEQ LLQQMKEHIG
SSLIISGKAL ILKHVYVERK MTPLNLYIND CDSKALAQVM LDYGRAIKDL AGANIFPGDM
LMKNFGVTRW GRVVFYDYDE ICPLTDCNFR EVPQTQNALE ELSSDSYFDI EPNDIFPSQF
KVFFSANELA FNAFNSHHSD LFNAQFWQTC QQQVQQGYLP DVYPYKQSWR FK
