(data stored in SCRATCH zone)

SWISSPROT: B7UIL6_ECO27

ID   B7UIL6_ECO27            Unreviewed;       241 AA.
AC   B7UIL6;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 72.
DE   RecName: Full=Uridylate kinase {ECO:0000256|HAMAP-Rule:MF_01220};
DE            Short=UK {ECO:0000256|HAMAP-Rule:MF_01220};
DE            EC=2.7.4.22 {ECO:0000256|HAMAP-Rule:MF_01220};
DE   AltName: Full=Uridine monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_01220};
DE            Short=UMP kinase {ECO:0000256|HAMAP-Rule:MF_01220};
DE            Short=UMPK {ECO:0000256|HAMAP-Rule:MF_01220};
GN   Name=pyrH {ECO:0000256|HAMAP-Rule:MF_01220,
GN   ECO:0000313|EMBL:CAS07724.1};
GN   OrderedLocusNames=E2348C_0176 {ECO:0000313|EMBL:CAS07724.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07724.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07724.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP.
CC       {ECO:0000256|HAMAP-Rule:MF_01220, ECO:0000256|SAAS:SAAS01087336}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + UMP = ADP + UDP; Xref=Rhea:RHEA:24400,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:456216; EC=2.7.4.22; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01220, ECO:0000256|SAAS:SAAS01122072};
CC   -!- ACTIVITY REGULATION: Allosterically activated by GTP. Inhibited by
CC       UTP. {ECO:0000256|HAMAP-Rule:MF_01220}.
CC   -!- ACTIVITY REGULATION: Inhibited by UTP.
CC       {ECO:0000256|SAAS:SAAS01071959}.
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo
CC       pathway; UDP from UMP (UMPK route): step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01220, ECO:0000256|SAAS:SAAS00056421}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01220,
CC       ECO:0000256|SAAS:SAAS01087343}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01220,
CC       ECO:0000256|SAAS:SAAS00056429}.
CC   -!- SIMILARITY: Belongs to the UMP kinase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01220, ECO:0000256|SAAS:SAAS01087340}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01220}.
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DR   EMBL; FM180568; CAS07724.1; -; Genomic_DNA.
DR   RefSeq; WP_000224573.1; NC_011601.1.
DR   SMR; B7UIL6; -.
DR   EnsemblBacteria; CAS07724; CAS07724; E2348C_0176.
DR   KEGG; ecg:E2348C_0176; -.
DR   HOGENOM; HOG000047187; -.
DR   KO; K09903; -.
DR   OMA; PIIVFDM; -.
DR   BioCyc; ECOL574521:E2348C_RS00910-MONOMER; -.
DR   UniPathway; UPA00159; UER00275.
DR   Proteomes; UP000008205; 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   CDD; cd04254; AAK_UMPK-PyrH-Ec; 1.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   HAMAP; MF_01220_B; PyrH_B; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR011817; Uridylate_kinase.
DR   InterPro; IPR015963; Uridylate_kinase_bac.
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; B7UIL6.
DR   SWISS-2DPAGE; B7UIL6.
KW   Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_01220};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01220,
KW   ECO:0000256|SAAS:SAAS00056455};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01220,
KW   ECO:0000256|SAAS:SAAS00056495};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01220,
KW   ECO:0000256|SAAS:SAAS00056414, ECO:0000313|EMBL:CAS07724.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01220,
KW   ECO:0000256|SAAS:SAAS00056462};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01220,
KW   ECO:0000256|SAAS:SAAS00056469};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01220,
KW   ECO:0000256|SAAS:SAAS00056481}.
FT   DOMAIN       10    219       AA_kinase. {ECO:0000259|Pfam:PF00696}.
FT   NP_BIND      15     18       ATP. {ECO:0000256|HAMAP-Rule:MF_01220}.
FT   NP_BIND     138    145       UMP. {ECO:0000256|HAMAP-Rule:MF_01220}.
FT   REGION       23     28       Involved in allosteric activation by GTP.
FT                                {ECO:0000256|HAMAP-Rule:MF_01220}.
FT   BINDING      57     57       UMP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01220}.
FT   BINDING      58     58       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01220}.
FT   BINDING      62     62       ATP. {ECO:0000256|HAMAP-Rule:MF_01220}.
FT   BINDING      77     77       UMP. {ECO:0000256|HAMAP-Rule:MF_01220}.
FT   BINDING     165    165       ATP. {ECO:0000256|HAMAP-Rule:MF_01220}.
FT   BINDING     171    171       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01220}.
FT   BINDING     174    174       ATP. {ECO:0000256|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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