ID PYRH_STRP1 Reviewed; 242 AA. AC P65938; P59007; Q490H1; Q490H2; Q490H3; Q9A151; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 04-NOV-2026, entry version 142. 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=SPy_0462, M5005_Spy0377; GN ORFNames=M5005_Spy0378, M5005_Spy0379; OS Streptococcus pyogenes serotype M1. OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=301447; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700294 / SF370 / Serotype M1; RX PubMed=11296296; DOI=10.1073/pnas.071559398; RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K., RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P., RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X., RA Clifton S.W., Roe B.A., McLaughlin R.E.; RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes."; RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1; RX PubMed=16088826; DOI=10.1086/432514; RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K., RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P., RA Musser J.M.; RT "Evolutionary origin and emergence of a highly successful clone of serotype RT M1 group A Streptococcus involved multiple horizontal gene transfer RT events."; RL J. Infect. Dis. 192:771-782(2005). RN [3] RP SEQUENCE REVISION. RA Beres S.B., Musser J.M.; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. RN [4] RP X-RAY CRYSTALLOGRAPHY. RG New York structural genomics research consortium (NYSGRC); RT "Crystal structure of a putative uridylate kinase (UMP-kinase) from RT Streptococcus pyogenes."; RL Submitted (APR-2005) to the PDB data bank. CC -!- FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP. CC {ECO:0000255|HAMAP-Rule:MF_01220}. CC -!- CATALYTIC ACTIVITY: CC Reaction=UMP + ATP = UDP + ADP; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE004092; AAK33476.1; -; Genomic_DNA. DR EMBL; CP000017; AAZ50995.2; -; Genomic_DNA. DR PDB; 1Z9D; X-ray; 2.80 A; A/B/C=2-242. DR AlphaFoldDB; P65938; -. DR SMR; P65938; -. DR KEGG; spy:SPy_0462; -. DR KEGG; spz:M5005_Spy0377; -. DR PATRIC; fig|160490.10.peg.390; -. DR HOGENOM; CLU_033861_0_0_9; -. DR OMA; AADHMGM; -. DR UniPathway; UPA00159; UER00275. DR EvolutionaryTrace; P65938; -. DR Proteomes; UP000000750; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0033862; F:UMP kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0006225; P:UDP biosynthetic process; IEA:TreeGrafter. DR CDD; cd04254; AAK_UMPK-PyrH-Ec; 1. DR FunFam; 3.40.1160.10:FF:000019; Uridylate kinase; 1. DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 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 NCBIfam; TIGR02075; pyrH_bact; 1. DR PANTHER; PTHR42833; URIDYLATE KINASE; 1. DR PANTHER; PTHR42833:SF4; URIDYLATE KINASE PUMPKIN, CHLOROPLASTIC; 1. DR Pfam; PF00696; AA_kinase; 1. DR PIRSF; PIRSF005650; Uridylate_kin; 1. DR SUPFAM; SSF53633; Carbamate kinase-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Allosteric enzyme; ATP-binding; Cytoplasm; Kinase; KW Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome; KW Transferase. FT CHAIN 1..242 FT /note="Uridylate kinase" FT /id="PRO_0000143894" FT REGION 19..24 FT /note="Involved in allosteric activation by GTP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT BINDING 11..14 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT BINDING 53 FT /ligand="UMP" FT /ligand_id="ChEBI:CHEBI:57865" 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 58 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT BINDING 73 FT /ligand="UMP" FT /ligand_id="ChEBI:CHEBI:57865" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT BINDING 134..141 FT /ligand="UMP" FT /ligand_id="ChEBI:CHEBI:57865" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT BINDING 162 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT BINDING 168 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT BINDING 171 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT STRAND 6..12 FT /evidence="ECO:0007829|PDB:1Z9D" FT HELIX 14..17 FT /evidence="ECO:0007829|PDB:1Z9D" FT STRAND 20..24 FT /evidence="ECO:0007829|PDB:1Z9D" FT HELIX 27..41 FT /evidence="ECO:0007829|PDB:1Z9D" FT TURN 42..44 FT /evidence="ECO:0007829|PDB:1Z9D" FT STRAND 46..51 FT /evidence="ECO:0007829|PDB:1Z9D" FT TURN 54..56 FT /evidence="ECO:0007829|PDB:1Z9D" FT HELIX 59..65 FT /evidence="ECO:0007829|PDB:1Z9D" FT HELIX 69..92 FT /evidence="ECO:0007829|PDB:1Z9D" FT TURN 93..95 FT /evidence="ECO:0007829|PDB:1Z9D" FT STRAND 98..104 FT /evidence="ECO:0007829|PDB:1Z9D" FT TURN 107..109 FT /evidence="ECO:0007829|PDB:1Z9D" FT STRAND 110..112 FT /evidence="ECO:0007829|PDB:1Z9D" FT HELIX 115..123 FT /evidence="ECO:0007829|PDB:1Z9D" FT STRAND 127..132 FT /evidence="ECO:0007829|PDB:1Z9D" FT HELIX 141..151 FT /evidence="ECO:0007829|PDB:1Z9D" FT STRAND 155..163 FT /evidence="ECO:0007829|PDB:1Z9D" FT STRAND 168..170 FT /evidence="ECO:0007829|PDB:1Z9D" FT TURN 172..174 FT /evidence="ECO:0007829|PDB:1Z9D" FT STRAND 182..185 FT /evidence="ECO:0007829|PDB:1Z9D" FT HELIX 186..190 FT /evidence="ECO:0007829|PDB:1Z9D" FT TURN 191..193 FT /evidence="ECO:0007829|PDB:1Z9D" FT HELIX 199..207 FT /evidence="ECO:0007829|PDB:1Z9D" FT STRAND 211..216 FT /evidence="ECO:0007829|PDB:1Z9D" FT HELIX 222..227 FT /evidence="ECO:0007829|PDB:1Z9D" FT STRAND 233..237 FT /evidence="ECO:0007829|PDB:1Z9D" SQ SEQUENCE 242 AA; 25896 MW; B4517145A5160433 CRC64; MEPKYQRILI KLSGEALAGE KGVGIDIPTV QAIAKEIAEV HVSGVQIALV IGGGNLWRGE PAADAGMDRV QADYTGMLGT VMNALVMADS LQHYGVDTRV QTAIPMQNVA EPYIRGRALR HLEKNRIVVF GAGIGSPYFS TDTTAALRAA EIEADAILMA KNGVDGVYNA DPKKDANAVK FDELTHGEVI KRGLKIMDAT ASTLSMDNDI DLVVFNMNEA GNIQRVVFGE HIGTTVSNKV CD //