PYRH_HELPY
ID PYRH_HELPY Reviewed; 240 AA.
AC P56106;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=HP_0777;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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; AE000511; AAD07823.1; -; Genomic_DNA.
DR PIR; A64617; A64617.
DR RefSeq; NP_207570.1; NC_000915.1.
DR RefSeq; WP_001148056.1; NC_018939.1.
DR PDB; 4A7W; X-ray; 1.80 A; A/B=1-240.
DR PDB; 4A7X; X-ray; 2.49 A; A/B/C/D/E/F=1-240.
DR PDBsum; 4A7W; -.
DR PDBsum; 4A7X; -.
DR AlphaFoldDB; P56106; -.
DR SMR; P56106; -.
DR IntAct; P56106; 3.
DR STRING; 85962.C694_03990; -.
DR PaxDb; P56106; -.
DR DNASU; 900266; -.
DR EnsemblBacteria; AAD07823; AAD07823; HP_0777.
DR KEGG; hpy:HP_0777; -.
DR PATRIC; fig|85962.47.peg.829; -.
DR eggNOG; COG0528; Bacteria.
DR OMA; PIIVFDM; -.
DR PhylomeDB; P56106; -.
DR BRENDA; 2.7.4.22; 2604.
DR UniPathway; UPA00159; UER00275.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0033862; F:UMP kinase activity; IBA:GO_Central.
DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006225; P:UDP biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Pyrimidine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..240
FT /note="Uridylate kinase"
FT /id="PRO_0000143848"
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 76
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 137..144
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"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:4A7W"
FT HELIX 16..20
FT /evidence="ECO:0007829|PDB:4A7W"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:4A7W"
FT HELIX 29..44
FT /evidence="ECO:0007829|PDB:4A7W"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:4A7W"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:4A7W"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:4A7X"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:4A7X"
FT HELIX 72..96
FT /evidence="ECO:0007829|PDB:4A7W"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:4A7W"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:4A7W"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:4A7W"
FT HELIX 118..126
FT /evidence="ECO:0007829|PDB:4A7W"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:4A7W"
FT HELIX 144..154
FT /evidence="ECO:0007829|PDB:4A7W"
FT STRAND 158..172
FT /evidence="ECO:0007829|PDB:4A7W"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:4A7W"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:4A7W"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:4A7W"
FT HELIX 201..209
FT /evidence="ECO:0007829|PDB:4A7W"
FT STRAND 214..221
FT /evidence="ECO:0007829|PDB:4A7W"
FT HELIX 224..231
FT /evidence="ECO:0007829|PDB:4A7W"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:4A7W"
SQ SEQUENCE 240 AA; 26172 MW; F978BAD5BBCA5828 CRC64;
MQAKIKNKRV LVKFSGEALA GDNQFGIDIH VLDHIAKEIK SLVENDIEVG IVIGGGNIIR
GVSAAQGGII RRTSGDYMGM LATVINAVAM QEALEHIGLD TRVQSAIEIK EICESYIYRK
AIRHLEKGRV VIFGAGTGNP FFTTDTAATL RAIEIGSDLI IKATKVDGIY DKDPNKFKDA
KKLDTLSYND ALIGDIEVMD DTAISLAKDN KLPIVVCNMF KKGNLLQVIK HQQGVFSMVK
