(data stored in ACNUC7421 zone)

SWISSPROT: HPRK_PARXL

ID   HPRK_PARXL              Reviewed;         322 AA.
AC   Q145W4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 82.
DE   RecName: Full=HPr kinase/phosphorylase {ECO:0000255|HAMAP-Rule:MF_01249};
DE            Short=HPrK/P {ECO:0000255|HAMAP-Rule:MF_01249};
DE            EC=2.7.11.- {ECO:0000255|HAMAP-Rule:MF_01249};
DE            EC=2.7.4.- {ECO:0000255|HAMAP-Rule:MF_01249};
DE   AltName: Full=HPr(Ser) kinase/phosphorylase {ECO:0000255|HAMAP-Rule:MF_01249};
GN   Name=hprK {ECO:0000255|HAMAP-Rule:MF_01249};
GN   OrderedLocusNames=Bxeno_A0337; ORFNames=Bxe_A4125;
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: Catalyzes the ATP- as well as the pyrophosphate-
CC       dependent phosphorylation of a specific serine residue in HPr, a
CC       phosphocarrier protein of the phosphoenolpyruvate-dependent sugar
CC       phosphotransferase system (PTS). HprK/P also catalyzes the
CC       pyrophosphate-producing, inorganic phosphate-dependent
CC       dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-
CC       Ser-HPr). {ECO:0000255|HAMAP-Rule:MF_01249}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[HPr protein]-L-serine + ATP = [HPr protein]-O-phospho-L-
CC         serine + ADP + H(+); Xref=Rhea:RHEA:46600, Rhea:RHEA-COMP:11602,
CC         Rhea:RHEA-COMP:11603, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01249};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[HPr protein]-O-phospho-L-serine + H(+) + phosphate =
CC         [HPr protein]-L-serine + diphosphate; Xref=Rhea:RHEA:46604,
CC         Rhea:RHEA-COMP:11602, Rhea:RHEA-COMP:11603, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29999, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; Evidence={ECO:0000255|HAMAP-Rule:MF_01249};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01249};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01249}.
CC   -!- DOMAIN: The Walker A ATP-binding motif also binds Pi and PPi.
CC       {ECO:0000255|HAMAP-Rule:MF_01249}.
CC   -!- MISCELLANEOUS: Both phosphorylation and phosphorolysis are carried
CC       out by the same active site and suggest a common mechanism for
CC       both reactions. {ECO:0000255|HAMAP-Rule:MF_01249}.
CC   -!- SIMILARITY: Belongs to the HPrK/P family. {ECO:0000255|HAMAP-
CC       Rule:MF_01249}.
DR   EMBL; CP000270; ABE28875.1; -; Genomic_DNA.
DR   RefSeq; WP_011486706.1; NZ_CP008760.1.
DR   SMR; Q145W4; -.
DR   STRING; 266265.Bxe_A4125; -.
DR   EnsemblBacteria; ABE28875; ABE28875; Bxe_A4125.
DR   GeneID; 4003437; -.
DR   KEGG; bxb:DR64_1801; -.
DR   KEGG; bxe:Bxe_A4125; -.
DR   PATRIC; fig|266265.5.peg.357; -.
DR   eggNOG; ENOG4105D1C; Bacteria.
DR   eggNOG; COG1493; LUCA.
DR   HOGENOM; HOG000099173; -.
DR   KO; K06023; -.
DR   OMA; IQKPGLA; -.
DR   OrthoDB; 391150at2; -.
DR   BioCyc; BXEN266265:BXE_RS01690-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 1.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006109; P:regulation of carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01918; HprK_C; 1.
DR   Gene3D; 3.40.1390.20; -; 1.
DR   HAMAP; MF_01249; HPr_kinase; 1.
DR   InterPro; IPR003755; HPr(Ser)_kin/Pase.
DR   InterPro; IPR011104; Hpr_kin/Pase_C.
DR   InterPro; IPR011126; Hpr_kin/Pase_Hpr_N.
DR   InterPro; IPR028979; Ser_kin/Pase_Hpr-like_N_sf.
DR   PANTHER; PTHR30305:SF1; PTHR30305:SF1; 1.
DR   Pfam; PF07475; Hpr_kinase_C; 1.
DR   Pfam; PF02603; Hpr_kinase_N; 1.
DR   SUPFAM; SSF75138; SSF75138; 1.
DR   TIGRFAMs; TIGR00679; hpr-ser; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q145W4.
DR   SWISS-2DPAGE; Q145W4.
KW   ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding;
KW   Multifunctional enzyme; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    322       HPr kinase/phosphorylase.
FT                                /FTId=PRO_1000067141.
FT   NP_BIND     161    168       ATP. {ECO:0000255|HAMAP-Rule:MF_01249}.
FT   REGION      209    218       Important for the catalytic mechanism of
FT                                both phosphorylation and
FT                                dephosphorylation. {ECO:0000255|HAMAP-
FT                                Rule:MF_01249}.
FT   REGION      271    276       Important for the catalytic mechanism of
FT                                dephosphorylation. {ECO:0000255|HAMAP-
FT                                Rule:MF_01249}.
FT   ACT_SITE    146    146       {ECO:0000255|HAMAP-Rule:MF_01249}.
FT   ACT_SITE    167    167       {ECO:0000255|HAMAP-Rule:MF_01249}.
FT   ACT_SITE    185    185       Proton acceptor; for phosphorylation
FT                                activity. Proton donor; for
FT                                dephosphorylation activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_01249}.
FT   ACT_SITE    250    250       {ECO:0000255|HAMAP-Rule:MF_01249}.
FT   METAL       168    168       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01249}.
FT   METAL       210    210       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01249}.
SQ   SEQUENCE   322 AA;  35205 MW;  73E8B9BD222E1805 CRC64;
     MDTSSINAQS IFDDNAATLK LSWLTGHEGW ERGFSSESVA NATSSADLVG HLNLIHPNRI
     QVLGDAEIDY YKRQTDEDRS RHMAELIALE PPFLVVAGGV PAPPELVLRC TRSSTPLFTT
     PMSAAAVIDS LRLYMSRILA PRATLHGVFL DILGMGVLLT GDSGLGKSEL GLELISRGHG
     LVADDAVDFV RLGPDFVEGR CPPLLQNLLE VRGLGLLDIK TIFGETAVRR KMKLKLIVQL
     VRRPDGEFQR LPLESQTVDV LGLPISKVTI QVAAGRNLAV LVEAAVRNTI LQLRGIDTLR
     DFMDRQRLAM QDPDSQFPGK LI
//

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