ID PYRH_NEIMB Reviewed; 239 AA. AC P65932; Q9JQT5; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 02-SEP-2026, entry version 118. DE RecName: Full=Uridylate kinase; DE Short=UK; DE EC=2.7.4.22; DE AltName: Full=Uridine monophosphate kinase; DE Short=UMP kinase; DE Short=UMPK; GN Name=pyrH; OrderedLocusNames=NMB2103; OS Neisseria meningitidis serogroup B (strain ATCC BAA-335 / MC58). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-335 / MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M., RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D., RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V., RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M., RA Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP FUNCTION, ACTIVITY REGULATION, KINETIC PARAMETERS, IDENTIFICATION BY MASS RP SPECTROMETRY, AND SUBUNIT. RX PubMed=17210578; DOI=10.1074/jbc.m606963200; RA Evrin C., Straut M., Slavova-Azmanova N., Bucurenci N., Onu A., Assairi L., RA Ionescu M., Palibroda N., Barzu O., Gilles A.-M.; RT "Regulatory mechanisms differ in UMP kinases from Gram-negative and Gram- RT positive bacteria."; RL J. Biol. Chem. 282:7242-7253(2007). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RG New York structural genomics research consortium (NYSGRC); RT "Crystal structure analysis of uridylate kinase from Neisseria RT meningitidis."; RL Submitted (FEB-2005) to the PDB data bank. CC -!- FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP. CC {ECO:0000269|PubMed:17210578}. 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; CC -!- ACTIVITY REGULATION: Allosterically activated by GTP. Inhibited by UTP. CC {ECO:0000269|PubMed:17210578}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=2.98 mM for ATP (in the absence of GTP) CC {ECO:0000269|PubMed:17210578}; CC KM=0.83 mM for ATP (in the presence of GTP) CC {ECO:0000269|PubMed:17210578}; CC KM=8.7 uM for UMP {ECO:0000269|PubMed:17210578}; CC Vmax=35 umol/min/mg enzyme (in the absence of GTP) CC {ECO:0000269|PubMed:17210578}; CC Vmax=66 umol/min/mg enzyme (in the presence of GTP) CC {ECO:0000269|PubMed:17210578}; CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CC UDP from UMP (UMPK route): step 1/1. CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:17210578}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the UMP kinase family. {ECO:0000305}. 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; AE002098; AAF42420.1; -; Genomic_DNA. DR PIR; H81006; H81006. DR RefSeq; WP_002215090.1; NC_003112.2. DR PDB; 1YBD; X-ray; 2.60 A; A/B/C=1-239. DR AlphaFoldDB; P65932; -. DR SMR; P65932; -. DR FunCoup; P65932; 568. DR STRING; 122586.NMB2103; -. DR PaxDb; 122586-NMB2103; -. DR DNASU; 903933; -. DR KEGG; nme:NMB2103; -. DR PATRIC; fig|122586.8.peg.2685; -. DR HOGENOM; CLU_033861_0_0_4; -. DR InParanoid; P65932; -. DR OrthoDB; 9807458at2; -. DR BRENDA; 2.7.4.22; 3593. DR SABIO-RK; P65932; -. DR UniPathway; UPA00159; UER00275. DR EvolutionaryTrace; P65932; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. 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; IBA:GO_Central. DR CDD; cd04254; AAK_UMPK-PyrH-Ec; 1. DR FunFam; 3.40.1160.10:FF:000001; 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. DR PDBsum; 1YBD; -. 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..239 FT /note="Uridylate kinase" FT /id="PRO_0000143866" FT BINDING 13..16 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 55 FT /ligand="UMP" FT /ligand_id="ChEBI:CHEBI:57865" FT /evidence="ECO:0000250" FT BINDING 56 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 60 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 75 FT /ligand="UMP" FT /ligand_id="ChEBI:CHEBI:57865" FT /evidence="ECO:0000250" FT BINDING 136..143 FT /ligand="UMP" FT /ligand_id="ChEBI:CHEBI:57865" FT /evidence="ECO:0000250" FT BINDING 163 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 164 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 169 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 172 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT STRAND 8..14 FT /evidence="ECO:0007829|PDB:1YBD" FT HELIX 16..20 FT /evidence="ECO:0007829|PDB:1YBD" FT STRAND 23..26 FT /evidence="ECO:0007829|PDB:1YBD" FT HELIX 29..44 FT /evidence="ECO:0007829|PDB:1YBD" FT STRAND 48..53 FT /evidence="ECO:0007829|PDB:1YBD" FT HELIX 56..66 FT /evidence="ECO:0007829|PDB:1YBD" FT HELIX 71..95 FT /evidence="ECO:0007829|PDB:1YBD" FT STRAND 100..106 FT /evidence="ECO:0007829|PDB:1YBD" FT STRAND 108..111 FT /evidence="ECO:0007829|PDB:1YBD" FT HELIX 117..125 FT /evidence="ECO:0007829|PDB:1YBD" FT STRAND 129..134 FT /evidence="ECO:0007829|PDB:1YBD" FT HELIX 143..153 FT /evidence="ECO:0007829|PDB:1YBD" FT STRAND 157..162 FT /evidence="ECO:0007829|PDB:1YBD" FT STRAND 164..167 FT /evidence="ECO:0007829|PDB:1YBD" FT STRAND 169..171 FT /evidence="ECO:0007829|PDB:1YBD" FT HELIX 173..175 FT /evidence="ECO:0007829|PDB:1YBD" FT STRAND 183..186 FT /evidence="ECO:0007829|PDB:1YBD" FT HELIX 187..192 FT /evidence="ECO:0007829|PDB:1YBD" FT HELIX 200..208 FT /evidence="ECO:0007829|PDB:1YBD" FT STRAND 213..216 FT /evidence="ECO:0007829|PDB:1YBD" FT HELIX 223..229 FT /evidence="ECO:0007829|PDB:1YBD" FT STRAND 234..238 FT /evidence="ECO:0007829|PDB:1YBD" SQ SEQUENCE 239 AA; 25700 MW; CB08FD7E1AFBC5FE CRC64; MTQQIKYKRV LLKLSGESLM GSDPFGINHD TIVQTVGEIA EVVKMGVQVG IVVGGGNIFR GVSAQAGSMD RATADYMGMM ATVMNALALK DAFETLGIKA RVQSALSMQQ IAETYARPKA IQYLEEGKVV IFAAGTGNPF FTTDTAAALR GAEMNCDVML KATNVDGVYT ADPKKDPSAT RYETITFDEA LLKNLKVMDA TAFALCRERK LNIVVFGIAK EGSLKRVITG EDEGTLVHC //