(data stored in ACNUC7421 zone)

SWISSPROT: ACEK_PARXL

ID   ACEK_PARXL              Reviewed;         612 AA.
AC   Q146J2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   16-JAN-2019, entry version 72.
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=Bxeno_A0209; ORFNames=Bxe_A4253;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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; CP000270; ABE28747.1; -; Genomic_DNA.
DR   RefSeq; WP_011486591.1; NZ_CP008760.1.
DR   SMR; Q146J2; -.
DR   STRING; 266265.Bxe_A4253; -.
DR   PRIDE; Q146J2; -.
DR   EnsemblBacteria; ABE28747; ABE28747; Bxe_A4253.
DR   GeneID; 4004013; -.
DR   KEGG; bxb:DR64_1930; -.
DR   KEGG; bxe:Bxe_A4253; -.
DR   PATRIC; fig|266265.5.peg.218; -.
DR   eggNOG; ENOG4105VS7; Bacteria.
DR   eggNOG; COG4579; LUCA.
DR   HOGENOM; HOG000247673; -.
DR   KO; K00906; -.
DR   OMA; EPWYSVG; -.
DR   OrthoDB; 245269at2; -.
DR   BioCyc; BXEN266265:BXE_RS01035-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 1.
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; Q146J2.
DR   SWISS-2DPAGE; Q146J2.
KW   ATP-binding; Complete proteome; Cytoplasm; Glyoxylate bypass;
KW   Hydrolase; Kinase; Nucleotide-binding; Protein phosphatase;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase;
KW   Tricarboxylic acid cycle.
FT   CHAIN         1    612       Isocitrate dehydrogenase
FT                                kinase/phosphatase.
FT                                /FTId=PRO_0000259149.
FT   NP_BIND     327    333       ATP. {ECO:0000255|HAMAP-Rule:MF_00747}.
FT   ACT_SITE    383    383       {ECO:0000255|HAMAP-Rule:MF_00747}.
FT   BINDING     348    348       ATP. {ECO:0000255|HAMAP-Rule:MF_00747}.
SQ   SEQUENCE   612 AA;  70542 MW;  00164CFD1609E5D8 CRC64;
     MNHFPKLLSS QIGFDVAQTM LEGFDRHYRI FRDAAIHAKT LFEQADWHGL QKLARDRITS
     YDERVEECVE LLEDEYDAEN IDDEVWQQIK LHYIGLLTTH RQPECAETFF NSVCCKILHR
     SYFSNDFIFV RPAISTEYIE NDEPAAKPTY RAYYPGKDGL AATLERIVTN FQLEPPFEDL
     TRDVGCVMQA IQDAFGVFDE APNFQIHVLS SLFYRNKSAY IIGRIINGDL LMPFAVPLRH
     VKPGVLALDT VLLKRDQLLI IFSFSHSYFL VDMEVPSAYV EFLGTIMQGK PKAEIYTSVG
     LQKQGKNLFY RDLLHHLSHS SDQFIIAPGI KGLVMLVFTL PSFPYVFKLI KDSFPPPKET
     TRAQIKEKYQ LVKRHDRLGR MADTLEYSSV ALPVSRLDEA LVRELEKEVP SLIEYDGDSL
     VIRHMYIERR MVPLNLFLQN GNDEDIEHGI KEYGNAIKEL MQANIFPGDM LYKNFGVTRH
     GRVVFYDYDE IEYLTDCNVR AVPAPRNEED EMSGEPWYSV GPHDIFPETY GTFLLGDPRV
     RRSFMQHHAD FFDPALWQRH KDHLLKGELA DFFPYDGSVR FCMRYPERFA DAAGAASNEQ
     DAPDAGRSVR AA
//

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