ID A0A1Q7F7E9_9ARCH Unreviewed; 226 AA. AC A0A1Q7F7E9; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 07-OCT-2020, entry version 14. 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=AUH71_05405 {ECO:0000313|EMBL:OLC22852.1}; OS Thaumarchaeota archaeon 13_1_40CM_4_48_7. OC Archaea; Thaumarchaeota. OX NCBI_TaxID=1805396 {ECO:0000313|EMBL:OLC22852.1, ECO:0000313|Proteomes:UP000186289}; RN [1] {ECO:0000313|EMBL:OLC22852.1, ECO:0000313|Proteomes:UP000186289} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=27843720; RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A., RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C., RA Banfield J.F.; RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal RT heterotrophy are prevalent below the grass root zone."; RL PeerJ 4:E2687-E2687(2016). 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: Inhibited by UTP. {ECO:0000256|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: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|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:OLC22852.1}. 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; MNFA01000058; OLC22852.1; -; Genomic_DNA. DR UniPathway; UPA00159; UER00275. DR Proteomes; UP000186289; 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 Gene3D; 3.40.1160.10; -; 1. DR HAMAP; MF_01220_A; PyrH_A; 1. DR InterPro; IPR036393; AceGlu_kinase-like_sf. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR011817; Uridylate_kinase. DR InterPro; IPR011818; Uridylate_kinase_arch/spir. DR Pfam; PF00696; AA_kinase; 1. DR PIRSF; PIRSF005650; Uridylate_kin; 1. DR SUPFAM; SSF53633; SSF53633; 1. DR TIGRFAMs; TIGR02076; pyrH_arch; 1. PE 3: Inferred from homology; 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:OLC22852.1}; 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 6..204 FT /note="AA_kinase" FT /evidence="ECO:0000259|Pfam:PF00696" FT NP_BIND 10..14 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" FT NP_BIND 116..122 FT /note="UMP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" FT BINDING 46 FT /note="UMP; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" FT BINDING 47 FT /note="ATP; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" FT BINDING 51 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" FT BINDING 68 FT /note="UMP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" FT BINDING 142 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" FT BINDING 148 FT /note="ATP; via amide nitrogen and carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" FT BINDING 151 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" SQ SEQUENCE 226 AA; 23857 MW; F962EDE1D7244C05 CRC64; MGTKERVVIK LSGSLFGDNA ADELKKYARM LLEISSETQP VVVAGGGNVA RHYIKIARGF GSDEASLDIM GIEVSRLNAR LLIAALGDNA YPAVPSDLEQ VSQAADGGKI VVTGGLHPGQ STNATAALIA EKVKAKKFLN ATDVDGIYDS DPNKNKGAKL FKDITVKKCF ELLGSENSAA GTYDLMDIVA LKVIERSKIP TVVLKSDPST IKNAIANKAT GTRIIV //