(data stored in ACNUC7421 zone)

SWISSPROT: PYRH_ECO57

ID   PYRH_ECO57              Reviewed;         241 AA.
AC   P0A7F1; P29464;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   05-JUL-2017, entry version 82.
DE   RecName: Full=Uridylate kinase {ECO:0000255|HAMAP-Rule:MF_01220};
DE            Short=UK {ECO:0000255|HAMAP-Rule:MF_01220};
DE            EC=2.7.4.22 {ECO:0000255|HAMAP-Rule:MF_01220};
DE   AltName: Full=Uridine monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_01220};
DE            Short=UMP kinase {ECO:0000255|HAMAP-Rule:MF_01220};
DE            Short=UMPK {ECO:0000255|HAMAP-Rule:MF_01220};
GN   Name=pyrH {ECO:0000255|HAMAP-Rule:MF_01220};
GN   OrderedLocusNames=Z0182, ECs0173;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP.
CC       {ECO:0000255|HAMAP-Rule:MF_01220}.
CC   -!- CATALYTIC ACTIVITY: ATP + UMP = ADP + UDP. {ECO:0000255|HAMAP-
CC       Rule:MF_01220}.
CC   -!- ENZYME REGULATION: Allosterically activated by GTP. Inhibited by
CC       UTP. {ECO:0000255|HAMAP-Rule:MF_01220}.
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo
CC       pathway; UDP from UMP (UMPK route): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01220}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01220}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01220}.
CC   -!- SIMILARITY: Belongs to the UMP kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01220}.
DR   EMBL; AE005174; AAG54473.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33596.1; -; Genomic_DNA.
DR   PIR; E85501; E85501.
DR   PIR; E90650; E90650.
DR   RefSeq; NP_308200.1; NC_002695.1.
DR   RefSeq; WP_000224573.1; NZ_MWVM01000012.1.
DR   ProteinModelPortal; P0A7F1; -.
DR   SMR; P0A7F1; -.
DR   MINT; MINT-1222932; -.
DR   STRING; 155864.Z0182; -.
DR   EnsemblBacteria; AAG54473; AAG54473; Z0182.
DR   EnsemblBacteria; BAB33596; BAB33596; BAB33596.
DR   GeneID; 913857; -.
DR   KEGG; ece:Z0182; -.
DR   KEGG; ecs:ECs0173; -.
DR   PATRIC; fig|386585.9.peg.275; -.
DR   eggNOG; ENOG4105C41; Bacteria.
DR   eggNOG; COG0528; LUCA.
DR   HOGENOM; HOG000047187; -.
DR   KO; K09903; -.
DR   UniPathway; UPA00159; UER00275.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0033862; F:UMP kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01220_B; PyrH_B; 1.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR011817; Uridylate_kinase.
DR   InterPro; IPR015963; Uridylate_kinase_bac.
DR   PANTHER; PTHR42833:SF2; PTHR42833:SF2; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   PIRSF; PIRSF005650; Uridylate_kin; 1.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   TIGRFAMs; TIGR02075; pyrH_bact; 1.
PE   3: Inferred from homology;
DR   PRODOM; P0A7F1.
DR   SWISS-2DPAGE; P0A7F1.
KW   Allosteric enzyme; ATP-binding; Complete proteome; Cytoplasm; Kinase;
KW   Nucleotide-binding; Pyrimidine biosynthesis; Transferase.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    241       Uridylate kinase.
FT                                /FTId=PRO_0000143843.
FT   NP_BIND      15     18       ATP. {ECO:0000255|HAMAP-Rule:MF_01220}.
FT   NP_BIND     138    145       UMP. {ECO:0000255|HAMAP-Rule:MF_01220}.
FT   REGION       23     28       Involved in allosteric activation by GTP.
FT                                {ECO:0000255|HAMAP-Rule:MF_01220}.
FT   BINDING      57     57       UMP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01220}.
FT   BINDING      58     58       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01220}.
FT   BINDING      62     62       ATP. {ECO:0000255|HAMAP-Rule:MF_01220}.
FT   BINDING      77     77       UMP. {ECO:0000255|HAMAP-Rule:MF_01220}.
FT   BINDING     165    165       ATP. {ECO:0000255|HAMAP-Rule:MF_01220}.
FT   BINDING     171    171       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01220}.
FT   BINDING     174    174       ATP. {ECO:0000255|HAMAP-Rule:MF_01220}.
SQ   SEQUENCE   241 AA;  25970 MW;  82EFA75F7226E201 CRC64;
     MATNAKPVYK RILLKLSGEA LQGTEGFGID ASILDRMAQE IKELVELGIQ VGVVIGGGNL
     FRGAGLAKAG MNRVVGDHMG MLATVMNGLA MRDALHRAYV NARLMSAIPL NGVCDSYSWA
     EAISLLRNNR VVILSAGTGN PFFTTDSAAC LRGIEIEADV VLKATKVDGV FTADPAKDPT
     ATMYEQLTYS EVLEKELKVM DLAAFTLARD HKLPIRVFNM NKPGALRRVV MGEKEGTLIT
     E
//

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