PYRH_TROW8
ID PYRH_TROW8 Reviewed; 231 AA.
AC Q83HZ6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=TW320;
OS Tropheryma whipplei (strain TW08/27) (Whipple's bacillus).
OC Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX NCBI_TaxID=218496;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW08/27;
RX PubMed=12606174; DOI=10.1016/s0140-6736(03)12597-4;
RA Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G.,
RA Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A.,
RA Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J.,
RA Relman D.A.;
RT "Sequencing and analysis of the genome of the Whipple's disease bacterium
RT Tropheryma whipplei.";
RL Lancet 361:637-644(2003).
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: Inhibited by UTP. {ECO:0000255|HAMAP-
CC 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; BX251411; CAD66993.1; -; Genomic_DNA.
DR RefSeq; WP_011096273.1; NC_004551.1.
DR AlphaFoldDB; Q83HZ6; -.
DR SMR; Q83HZ6; -.
DR GeneID; 67388094; -.
DR KEGG; tws:TW320; -.
DR HOGENOM; CLU_033861_0_0_11; -.
DR OMA; PIIVFDM; -.
DR UniPathway; UPA00159; UER00275.
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 ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Pyrimidine biosynthesis; Transferase.
FT CHAIN 1..231
FT /note="Uridylate kinase"
FT /id="PRO_0000323978"
FT BINDING 9..12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 49
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 69
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 130..137
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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 167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
SQ SEQUENCE 231 AA; 24817 MW; D3FE706DC4AD62BF CRC64;
MASRRVLLKL SGESFGGGAP LVDPDVVSAI ASEIVRVSKT IQIAIVVGGG NYFRGAELSR
RGMARDRADY MGMLGTVINA LALQDFLEQA GGDTRVQSAI SMSQVAELYV PRRAERHLTK
GRVVIFAAGA GMPYFSTDTV AVQRALEIKA DIVLIAKNGV DGVYTDDPQI NPNAKKIYKI
TYREALERGL RVVDSAALGL CMEHGLPMRV FGMESLRDAV SGLKVGTELS Q
