(data stored in ACNUC7421 zone)

SWISSPROT: ACEK_RHOPS

ID   ACEK_RHOPS              Reviewed;         606 AA.
AC   Q13E74;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   16-JAN-2019, entry version 76.
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};
GN   OrderedLocusNames=RPD_0377;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Bifunctional enzyme which can phosphorylate or
CC       dephosphorylate isocitrate dehydrogenase (IDH) on a specific
CC       serine residue. This is a regulatory mechanism which enables
CC       bacteria to bypass the Krebs cycle via the glyoxylate shunt in
CC       response to the source of carbon. When bacteria are grown on
CC       glucose, IDH is fully active and unphosphorylated, but when grown
CC       on acetate or ethanol, the activity of IDH declines drastically
CC       concomitant with its phosphorylation. {ECO:0000255|HAMAP-
CC       Rule:MF_00747}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[isocitrate dehydrogenase]-L-serine + ATP = [isocitrate
CC         dehydrogenase]-O-phospho-L-serine + ADP + H(+);
CC         Xref=Rhea:RHEA:43540, Rhea:RHEA-COMP:10605, Rhea:RHEA-
CC         COMP:10606, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         EC=2.7.11.5; Evidence={ECO:0000255|HAMAP-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}.
DR   EMBL; CP000283; ABE37615.1; -; Genomic_DNA.
DR   RefSeq; WP_011500803.1; NC_007958.1.
DR   SMR; Q13E74; -.
DR   STRING; 316057.RPD_0377; -.
DR   EnsemblBacteria; ABE37615; ABE37615; RPD_0377.
DR   KEGG; rpd:RPD_0377; -.
DR   eggNOG; ENOG4105VS7; Bacteria.
DR   eggNOG; COG4579; LUCA.
DR   HOGENOM; HOG000033780; -.
DR   KO; K00906; -.
DR   OMA; EPWYSVG; -.
DR   OrthoDB; 245269at2; -.
DR   BioCyc; RPAL316057:RPD_RS01945-MONOMER; -.
DR   Proteomes; UP000001818; Chromosome.
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: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.
DR   ProDom; PD043552; Isocitrate_DH_AceK; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13E74.
DR   SWISS-2DPAGE; Q13E74.
KW   ATP-binding; Complete proteome; Cytoplasm; Glyoxylate bypass;
KW   Hydrolase; Kinase; Nucleotide-binding; Protein phosphatase;
KW   Serine/threonine-protein kinase; Transferase;
KW   Tricarboxylic acid cycle.
FT   CHAIN         1    606       Isocitrate dehydrogenase
FT                                kinase/phosphatase.
FT                                /FTId=PRO_0000288299.
FT   NP_BIND     354    360       ATP. {ECO:0000255|HAMAP-Rule:MF_00747}.
FT   ACT_SITE    414    414       {ECO:0000255|HAMAP-Rule:MF_00747}.
FT   BINDING     375    375       ATP. {ECO:0000255|HAMAP-Rule:MF_00747}.
SQ   SEQUENCE   606 AA;  67370 MW;  3684B16E8958EA11 CRC64;
     MTADAHLFSA SDLEAATRIA EPDFELLDAL IRTDDPDDQA HTLARVALSA FDNYYAVSRR
     IPALAKAAFY ARDWPATVRL SKIRIGLYTA CIDQLVPLLK AGLPELANDE QVWVRAEAEL
     LAAIAGRYEA DFAFAFWQSL RRKLVSDEWR PVSYDTGPAA RPPAAIAAVV RTIAATLPIQ
     PEVIRNVLDA AGFTGPWRDL DGDAALAAAA IEAALEPLSP RAGETAKIEI AESGFFRNRG
     ACLVGRIRLR DRGDMPPRNI PLLVALLNED DGLVVDAVLC DSDELQFAFS STLANYHATN
     PRYHELARLL HELMPKRPLG TQYSCIGFHH LGKVAVMNEI LTEHRRSKEK LATAPGFKGT
     VAIAFTMPCS AYVLKIIRDH PTDDYKFDYF DGLDAVLRKY NLVHEIDRAG SMLDNIIYSN
     VKLARTMFAP DLLDELLEAG IGTVTLERDA LVFRHLIVQI KLTPLPLYLT TAAAADARAA
     VINLGDCIKN NAAADIFNKD LDGRNYGVSR IRKVYLFDYD AVEQLTEVKV RSTPPMPRAE
     DEDGVVFRPA QMLEGLRIDD PGLRRAFRDA HPELMQPDYW EGMQHALRAG KVPKVMNYPT
     SRRLRR
//

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