ID H3CNB9_TETNG Unreviewed; 265 AA.
AC H3CNB9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Uridine-cytidine kinase {ECO:0000256|RuleBase:RU003825};
DE EC=2.7.1.48 {ECO:0000256|RuleBase:RU003825};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000009750.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000009750.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cytidine = ADP + CMP + H(+); Xref=Rhea:RHEA:24674,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17562, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.1.48;
CC Evidence={ECO:0000256|ARBA:ARBA00000503,
CC ECO:0000256|RuleBase:RU003825};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + uridine = ADP + H(+) + UMP; Xref=Rhea:RHEA:16825,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16704, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57865, ChEBI:CHEBI:456216; EC=2.7.1.48;
CC Evidence={ECO:0000256|ARBA:ARBA00000734,
CC ECO:0000256|RuleBase:RU003825};
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway;
CC CTP from cytidine: step 1/3. {ECO:0000256|RuleBase:RU003825}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC UMP from uridine: step 1/1. {ECO:0000256|ARBA:ARBA00004690,
CC ECO:0000256|RuleBase:RU003825}.
CC -!- SIMILARITY: Belongs to the uridine kinase family.
CC {ECO:0000256|ARBA:ARBA00005408, ECO:0000256|RuleBase:RU003825}.
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DR AlphaFoldDB; H3CNB9; -.
DR STRING; 99883.ENSTNIP00000009750; -.
DR Ensembl; ENSTNIT00000009926.1; ENSTNIP00000009750.1; ENSTNIG00000006951.1.
DR GeneTree; ENSGT01020000230412; -.
DR HOGENOM; CLU_021278_1_1_1; -.
DR InParanoid; H3CNB9; -.
DR OMA; TVKPMHE; -.
DR TreeFam; TF316686; -.
DR UniPathway; UPA00574; UER00637.
DR UniPathway; UPA00579; UER00640.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043771; F:cytidine kinase activity; IEA:RHEA.
DR GO; GO:0004849; F:uridine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0044211; P:CTP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR CDD; cd02023; UMPK; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006083; PRK/URK.
DR InterPro; IPR000764; Uridine_kinase-like.
DR NCBIfam; TIGR00235; udk; 1.
DR PANTHER; PTHR10285; URIDINE KINASE; 1.
DR PANTHER; PTHR10285:SF147; URIDINE-CYTIDINE KINASE 2-B; 1.
DR Pfam; PF00485; PRK; 1.
DR PRINTS; PR00988; URIDINKINASE.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003825};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003825};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003825};
KW Reference proteome {ECO:0000313|Proteomes:UP000007303};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003825}.
FT DOMAIN 27..222
FT /note="Phosphoribulokinase/uridine kinase"
FT /evidence="ECO:0000259|Pfam:PF00485"
FT REGION 241..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 265 AA; 30057 MW; 19B4D63B442E71B5 CRC64;
IASMAGDSET HLRSGDESTD IIRQPFLIGV SGGTASGKSS VCEKIMELLG QNKIDHHQRQ
VAILSQDSFY KVLTPEQKAK AVKGQFNFDH PDAFDNDLVL QTLQDILQGK TVQIPVYDFV
THSRKDEFVT VYPADVVLFE GILMFYAQEI RDMFQMKLFV DTDPYTRLSR RVLRDISERG
RELEQVLNQY ITFVKPAFEE FCLPTKKYAD VIIPRGADNL VAINLIVQHI QDILNGGLNK
RQNGYVNGHS TPRQRRASES SSRPH
//
