(data stored in ACNUC9543 zone)

SWISSPROT: PYRH_YERPA

ID   PYRH_YERPA              Reviewed;         241 AA.
AC   Q1CAN2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   08-MAY-2019, entry version 83.
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=YPA_0522;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP.
CC       {ECO:0000255|HAMAP-Rule:MF_01220}.
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:0000255|HAMAP-
CC         Rule:MF_01220};
CC   -!- ACTIVITY 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; CP000308; ABG12490.1; -; Genomic_DNA.
DR   RefSeq; WP_002212133.1; NZ_CP009906.1.
DR   SMR; Q1CAN2; -.
DR   EnsemblBacteria; ABG12490; ABG12490; YPA_0522.
DR   KEGG; ypa:YPA_0522; -.
DR   HOGENOM; HOG000047187; -.
DR   KO; K09903; -.
DR   OMA; PIIVFDM; -.
DR   UniPathway; UPA00159; UER00275.
DR   Proteomes; UP000001971; 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; Q1CAN2.
DR   SWISS-2DPAGE; Q1CAN2.
KW   Allosteric enzyme; ATP-binding; Complete proteome; Cytoplasm; Kinase;
KW   Nucleotide-binding; Pyrimidine biosynthesis; Transferase.
FT   CHAIN         1    241       Uridylate kinase.
FT                                /FTId=PRO_1000054056.
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;  25973 MW;  C9CCDC5E3F95A0C4 CRC64;
     MATNAKPVYQ RILLKLSGEA LQGAEGFGID ASVLDRMAQE VKELVELGIQ VGVVIGGGNL
     FRGAGLAQAG MNRVVGDHMG MLATVMNGLA MRDALHRAYV NARLMSAIPL NGVCDNYSWA
     EAISLLRHNR VVIFAAGTGN PFFTTDSAAC LRGIEIEADV VLKATKVDGV YSADPVKNPD
     ATLYEQLTYQ DVLEQELKVM DLAAFTLARD HNLPIRVFNM NKPGALRRVV MGENEGTLIA
     K
//

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