ID A0A3P9BBH7_9CICH Unreviewed; 207 AA. AC A0A3P9BBH7; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 27-MAR-2024, entry version 22. DE RecName: Full=UMP-CMP kinase {ECO:0000256|HAMAP-Rule:MF_03172}; DE EC=2.7.4.14 {ECO:0000256|HAMAP-Rule:MF_03172}; DE AltName: Full=Deoxycytidylate kinase {ECO:0000256|HAMAP-Rule:MF_03172}; DE Short=CK {ECO:0000256|HAMAP-Rule:MF_03172}; DE Short=dCMP kinase {ECO:0000256|HAMAP-Rule:MF_03172}; DE AltName: Full=Nucleoside-diphosphate kinase {ECO:0000256|HAMAP-Rule:MF_03172}; DE EC=2.7.4.6 {ECO:0000256|HAMAP-Rule:MF_03172}; DE AltName: Full=Uridine monophosphate/cytidine monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_03172}; DE Short=UMP/CMP kinase {ECO:0000256|HAMAP-Rule:MF_03172}; DE Short=UMP/CMPK {ECO:0000256|HAMAP-Rule:MF_03172}; GN Name=CMPK1 {ECO:0000256|HAMAP-Rule:MF_03172, GN ECO:0000313|Ensembl:ENSMZEP00005007136.1}; GN Synonyms=CMPK {ECO:0000256|HAMAP-Rule:MF_03172}; OS Maylandia zebra (zebra mbuna). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids; OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex. OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005007136.1, ECO:0000313|Proteomes:UP000265160}; RN [1] {ECO:0000313|Ensembl:ENSMZEP00005007136.1, ECO:0000313|Proteomes:UP000265160} RP NUCLEOTIDE SEQUENCE. RX PubMed=25186727; DOI=10.1038/nature13726; RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S., RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J., RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C., RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R., RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F., RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W., RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M., RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H., RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P., RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E., RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S., RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O., RA Di Palma F.; RT "The genomic substrate for adaptive radiation in African cichlid fish."; RL Nature 513:375-381(2014). RN [2] {ECO:0000313|Ensembl:ENSMZEP00005007136.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2023) to UniProtKB. CC -!- FUNCTION: Catalyzes the phosphorylation of pyrimidine nucleoside CC monophosphates at the expense of ATP. Plays an important role in de CC novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP CC as phosphate acceptors. Also displays broad nucleoside diphosphate CC kinase activity. {ECO:0000256|HAMAP-Rule:MF_03172}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, CC ChEBI:CHEBI:456216; EC=2.7.4.14; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03172}; 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=2.7.4.14; CC Evidence={ECO:0000256|ARBA:ARBA00001331, ECO:0000256|HAMAP- CC Rule:MF_03172}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, CC ChEBI:CHEBI:456216; EC=2.7.4.14; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03172}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'- CC deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, CC ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03172}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'- CC triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03172}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03172}; CC Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000256|HAMAP-Rule:MF_03172}; CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP- CC Rule:MF_03172}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_03172}. Nucleus {ECO:0000256|HAMAP- CC Rule:MF_03172}. Note=Predominantly nuclear. {ECO:0000256|HAMAP- CC Rule:MF_03172}. CC -!- DOMAIN: Consists of three domains, a large central CORE domain and two CC small peripheral domains, NMPbind and LID, which undergo movements CC during catalysis. The LID domain closes over the site of phosphoryl CC transfer upon ATP binding. Assembling and dissambling the active center CC during each catalytic cycle provides an effective means to prevent ATP CC hydrolysis. {ECO:0000256|HAMAP-Rule:MF_03172}. CC -!- SIMILARITY: Belongs to the adenylate kinase family. UMP-CMP kinase CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03172}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03172}. 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 AlphaFoldDB; A0A3P9BBH7; -. DR STRING; 106582.ENSMZEP00005007136; -. DR Ensembl; ENSMZET00005007445.1; ENSMZEP00005007136.1; ENSMZEG00005005486.1. DR GeneTree; ENSGT00940000160589; -. DR Proteomes; UP000265160; LG18. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0036430; F:CMP kinase activity; IEA:RHEA. DR GO; GO:0036431; F:dCMP kinase activity; IEA:RHEA. DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0033862; F:UMP kinase activity; IEA:RHEA. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd01428; ADK; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1. DR HAMAP; MF_03172; Adenylate_kinase_UMP_CMP_kin; 1. DR InterPro; IPR000850; Adenylat/UMP-CMP_kin. DR InterPro; IPR033690; Adenylat_kinase_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR006266; UMP_CMP_kinase. DR NCBIfam; TIGR01359; UMP_CMP_kin_fam; 1. DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1. DR PANTHER; PTHR23359:SF206; UMP-CMP KINASE; 1. DR Pfam; PF00406; ADK; 1. DR PRINTS; PR00094; ADENYLTKNASE. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00113; ADENYLATE_KINASE; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_03172}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03172}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03172}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03172}; KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03172}; KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP- KW Rule:MF_03172}; Reference proteome {ECO:0000313|Proteomes:UP000265160}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_03172}. FT REGION 144..154 FT /note="LID" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172" FT BINDING 36..41 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172" FT BINDING 72..74 FT /ligand="a ribonucleoside 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:58043" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172" FT BINDING 104..107 FT /ligand="a ribonucleoside 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:58043" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172" FT BINDING 111 FT /ligand="CMP" FT /ligand_id="ChEBI:CHEBI:60377" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172" FT BINDING 145 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172" FT BINDING 151 FT /ligand="a ribonucleoside 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:58043" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172" FT BINDING 162 FT /ligand="a ribonucleoside 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:58043" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172" FT BINDING 190 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172" SQ SEQUENCE 207 AA; 23363 MW; 36BC55E2CF418034 CRC64; MIGRLFGNLS QKVPSLLYRV SLVMKPQVVF VLGGPGAGKG TQCSKIVESY GYTHLEESEF GQLIANYIKE GKIVPVEITI NLLRKAMEAT MKENENKFRF LIDGFPRNED NLQGWNSVMD GKADVKFVLF FDCSNEVCIN RCLERGKSSG RTDDNRESLE KRIQTYLQST RPIIDLYEKQ GKVHTIDASR SVDEVFADVK AILDKEG //