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Database: UniProt
Entry: A0A2U1PA37_ARTAN
LinkDB: A0A2U1PA37_ARTAN
Original site: A0A2U1PA37_ARTAN 
ID   A0A2U1PA37_ARTAN        Unreviewed;       895 AA.
AC   A0A2U1PA37;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Uridine kinase {ECO:0000256|RuleBase:RU003825};
DE            EC=2.7.1.48 {ECO:0000256|RuleBase:RU003825};
GN   ORFNames=CTI12_AA174060 {ECO:0000313|EMBL:PWA82616.1};
OS   Artemisia annua (Sweet wormwood).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC   Artemisiinae; Artemisia.
OX   NCBI_TaxID=35608 {ECO:0000313|EMBL:PWA82616.1, ECO:0000313|Proteomes:UP000245207};
RN   [1] {ECO:0000313|EMBL:PWA82616.1, ECO:0000313|Proteomes:UP000245207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Huhao1 {ECO:0000313|Proteomes:UP000245207};
RC   TISSUE=Leaf {ECO:0000313|EMBL:PWA82616.1};
RX   PubMed=29703587; DOI=10.1016/j.molp.2018.03.015;
RA   Shen Q., Zhang L., Liao Z., Wang S., Yan T., Shi P., Liu M., Fu X., Pan Q.,
RA   Wang Y., Lv Z., Lu X., Zhang F., Jiang W., Ma Y., Chen M., Hao X., Li L.,
RA   Tang Y., Lv G., Zhou Y., Sun X., Brodelius P.E., Rose J.K.C., Tang K.;
RT   "The genome of Artemisia annua provides insight into the evolution of
RT   Asteraceae family and artemisinin biosynthesis.";
RL   Mol. Plant 11:776-788(2018).
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|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|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|RuleBase:RU003825}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the UPRTase family.
CC       {ECO:0000256|ARBA:ARBA00010723}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the uridine kinase
CC       family. {ECO:0000256|ARBA:ARBA00008173}.
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:PWA82616.1}.
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DR   EMBL; PKPP01001453; PWA82616.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U1PA37; -.
DR   STRING; 35608.A0A2U1PA37; -.
DR   UniPathway; UPA00574; UER00637.
DR   UniPathway; UPA00579; UER00640.
DR   Proteomes; UP000245207; 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:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-EC.
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; cd06223; PRTases_typeI; 1.
DR   CDD; cd02023; UMPK; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR015410; DUF1985.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR006083; PRK/URK.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR000764; Uridine_kinase-like.
DR   NCBIfam; TIGR00235; udk; 1.
DR   PANTHER; PTHR10285; URIDINE KINASE; 1.
DR   PANTHER; PTHR10285:SF97; URIDINE KINASE-LIKE PROTEIN 3; 1.
DR   Pfam; PF09331; DUF1985; 1.
DR   Pfam; PF00485; PRK; 1.
DR   Pfam; PF14681; UPRTase; 1.
DR   PRINTS; PR00988; URIDINKINASE.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW   ATP-binding {ECO:0000256|RuleBase:RU003825};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
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:UP000245207};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003825}.
FT   DOMAIN          75..200
FT                   /note="DUF1985"
FT                   /evidence="ECO:0000259|Pfam:PF09331"
FT   DOMAIN          478..661
FT                   /note="Phosphoribulokinase/uridine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00485"
SQ   SEQUENCE   895 AA;  101731 MW;  900AF10EE84386CE CRC64;
     MSELGISEVV LYDAKLTIRA QIAIASDIRT KLINTPRYAL FRETCFGPWL DVQLTYKNPS
     LVHLILQTEY IPEQPKNDEI LFRVGGHELR FGREEFCLIT GFRFGTIKPS SEGSCHIPFR
     DRVFSHIPGK ISIKGSDVAS IFKDSFDQIS DLDAVRICLL LLLEIGFIGR QPNFVIDEEL
     LRLVEDLDSW NTFPWGSYIW NVTYPQLAGA LQTRRGLHLS NLATKEAKYT LVGFIWAFKI
     WILEVFPAAR KFAVRDPGVI PRAIAWRSTC TIKKEMLHNF LVFKEGLEPL HELIPTLAES
     STPWWMASRR FFDGIVDDFQ PPLKKLRFTA PPSPLEPHSQ HAMVLYPNHA ERSRSGTTAS
     HHTMEERIME KVVKMIDHPV SRKEELVEEL SKDRRSPEVH TEMPKMSDFV DEMASEPILR
     LKERVKVESR VLHSLPDFSD RVYCASDGVE GNRTGTRNTN VEQASTSVTG KSHKQPFVIG
     VAGGAASGKT VVCNLIIEQL HDLRVVLVKQ ESFYHNLTSK ELSEFHEYNF DHPDAFNTEK
     VLTAMEMLKY GKAIDIPEYD FKSHKTGVPR RVNPSDVVIL EGILILYDPR VRDMMDMKIF
     VDTDADVRLE RRIRRDTGER GRDISLVLGQ YSKFVKPAFD AFILPTKKYA DIIIPHEGDN
     HLTIDLIGQH VQTKLGQHDL CKIYPNLYVI QSTFQIRAMH TLIRDFQTTQ DDFTFHADRL
     IRMVVEHGLG HLPFTEKQVT TPTGSVYTGV DFDKSLCGVS VIRSGESMET ALRACCKGIK
     IGKILIHKEG ENGHQVIYER LPQDISDRHV LLLDPILGTG YSAVEAINLL LKRGVPEGNI
     IFLNLISAPQ GVHVVCKRFP RIKIVTSEIE TGLNQESRVI PGMGEFGDRY FGTEF
//
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