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PYRH_STAS1
ID   PYRH_STAS1              Reviewed;         240 AA.
AC   Q49X43;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
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}; OrderedLocusNames=SSP1510;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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 UTP.
CC       {ECO:0000255|HAMAP-Rule:MF_01220}.
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC       UDP from UMP (UMPK route): step 1/1. {ECO:0000255|HAMAP-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}.
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DR   EMBL; AP008934; BAE18655.1; -; Genomic_DNA.
DR   RefSeq; WP_002483465.1; NZ_MTGA01000034.1.
DR   AlphaFoldDB; Q49X43; -.
DR   SMR; Q49X43; -.
DR   STRING; 342451.SSP1510; -.
DR   EnsemblBacteria; BAE18655; BAE18655; SSP1510.
DR   KEGG; ssp:SSP1510; -.
DR   eggNOG; COG0528; Bacteria.
DR   HOGENOM; CLU_033861_0_0_9; -.
DR   OMA; PIIVFDM; -.
DR   OrthoDB; 1043239at2; -.
DR   UniPathway; UPA00159; UER00275.
DR   Proteomes; UP000006371; 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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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;
KW   Allosteric enzyme; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Pyrimidine biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..240
FT                   /note="Uridylate kinase"
FT                   /id="PRO_0000143890"
FT   REGION          21..26
FT                   /note="Involved in allosteric activation by GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         13..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         55
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         56
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         60
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         75
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         136..143
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         164
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         170
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         173
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
SQ   SEQUENCE   240 AA;  26083 MW;  1C2AC8BEA2E89F40 CRC64;
     MAQTSKYERV VLKLSGEALA GDDGFGINPI IIKSIAEQVA EVAKLDCEIA VIVGGGNIWR
     GKTGSDLGMD RGTADYMGML ATVMNALALQ DSLEQLECDT RVLTSIEMKQ VAEPYIRRRA
     IRHLEKNRVV IFAAGIGNPY FSTDTTAALR AAEVEADVIL MGKNNVDGVY SADPKVDPNA
     IKYEHLTHIQ MLQEGLQVMD STASSFCMDN NIPLNVFSIT EEGNIKRAVM GEKIGTLITK
 
 
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