ID A0A1V4AGP1_9BACT Unreviewed; 237 AA. AC A0A1V4AGP1; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 29-SEP-2021, entry version 15. DE RecName: Full=Uridylate kinase {ECO:0000256|HAMAP-Rule:MF_01220}; DE Short=UK {ECO:0000256|HAMAP-Rule:MF_01220}; DE EC=2.7.4.22 {ECO:0000256|HAMAP-Rule:MF_01220}; DE AltName: Full=Uridine monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_01220}; DE Short=UMP kinase {ECO:0000256|HAMAP-Rule:MF_01220}; DE Short=UMPK {ECO:0000256|HAMAP-Rule:MF_01220}; GN Name=pyrH {ECO:0000256|HAMAP-Rule:MF_01220}; GN ORFNames=B0D78_11920 {ECO:0000313|EMBL:OON86226.1}; OS Pyramidobacter sp. C12-8. OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Pyramidobacter; unclassified Pyramidobacter. OX NCBI_TaxID=1943580 {ECO:0000313|EMBL:OON86226.1, ECO:0000313|Proteomes:UP000190264}; RN [1] {ECO:0000313|EMBL:OON86226.1, ECO:0000313|Proteomes:UP000190264} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C12-8 {ECO:0000313|EMBL:OON86226.1, RC ECO:0000313|Proteomes:UP000190264}; RA Kang S.; RT "Fluoroacetate degrading rumen bacteria."; RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP. CC {ECO:0000256|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; CC Evidence={ECO:0000256|ARBA:ARBA00001018, ECO:0000256|HAMAP- CC Rule:MF_01220}; CC -!- ACTIVITY REGULATION: Allosterically activated by GTP. Inhibited by UTP. CC {ECO:0000256|HAMAP-Rule:MF_01220}. CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CC UDP from UMP (UMPK route): step 1/1. {ECO:0000256|ARBA:ARBA00004791, CC ECO:0000256|HAMAP-Rule:MF_01220}. CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01220}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_01220}. CC -!- SIMILARITY: Belongs to the UMP kinase family. CC {ECO:0000256|ARBA:ARBA00007614, ECO:0000256|HAMAP-Rule:MF_01220}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01220}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:OON86226.1}. 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; MUHX01000048; OON86226.1; -; Genomic_DNA. DR EnsemblBacteria; OON86226; OON86226; B0D78_11920. DR UniPathway; UPA00159; UER00275. DR Proteomes; UP000190264; Unassembled WGS sequence. 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 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 {ECO:0000256|HAMAP-Rule:MF_01220}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01220}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01220}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_01220, ECO:0000313|EMBL:OON86226.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01220}; KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP- KW Rule:MF_01220}; Transferase {ECO:0000256|HAMAP-Rule:MF_01220}. FT DOMAIN 4..214 FT /note="AA_kinase" FT /evidence="ECO:0000259|Pfam:PF00696" FT NP_BIND 9..12 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" FT NP_BIND 133..140 FT /note="UMP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" FT REGION 17..22 FT /note="Involved in allosteric activation by GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" FT BINDING 51 FT /note="UMP; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" FT BINDING 52 FT /note="ATP; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" FT BINDING 56 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" FT BINDING 71 FT /note="UMP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" FT BINDING 160 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" FT BINDING 166 FT /note="ATP; via amide nitrogen and carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" FT BINDING 169 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" SQ SEQUENCE 237 AA; 25978 MW; 4CAC9E7A7B5E39B9 CRC64; MKFKRVLLKL SGEVLAGPQG FGLDFRAIDR MCRQIAQVAA DGIQIGLVVG GGNFFRGRQA VDEGVERSQA DYMGMLGTVI NALALQDVLE RKNDIPTRVL TAIEMRQVAE PYIRRRALRH IEKGRVVIFA AGTGSPYFST DTTAALRAAE IGAECLVKAT KVDGIYDKDP FKYSDAVKFE KLSYMDALQR RIEVMDAAAF SLCMENGIPI AVLNVLEEGS LRAFLIEGKN IGTIVSK //