ID A0A0D2VFM6_GOSRA Unreviewed; 479 AA.
AC A0A0D2VFM6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Uridine kinase {ECO:0000256|RuleBase:RU003825};
DE EC=2.7.1.48 {ECO:0000256|RuleBase:RU003825};
GN ORFNames=B456_013G150100 {ECO:0000313|EMBL:KJB81524.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB81524.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB81524.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
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}.
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DR EMBL; CM001752; KJB81519.1; -; Genomic_DNA.
DR EMBL; CM001752; KJB81522.1; -; Genomic_DNA.
DR EMBL; CM001752; KJB81523.1; -; Genomic_DNA.
DR EMBL; CM001752; KJB81524.1; -; Genomic_DNA.
DR RefSeq; XP_012463743.1; XM_012608289.1.
DR RefSeq; XP_012463745.1; XM_012608291.1.
DR RefSeq; XP_012463746.1; XM_012608292.1.
DR AlphaFoldDB; A0A0D2VFM6; -.
DR STRING; 29730.A0A0D2VFM6; -.
DR EnsemblPlants; KJB81519; KJB81519; B456_013G150100.
DR EnsemblPlants; KJB81522; KJB81522; B456_013G150100.
DR EnsemblPlants; KJB81523; KJB81523; B456_013G150100.
DR EnsemblPlants; KJB81524; KJB81524; B456_013G150100.
DR GeneID; 105783095; -.
DR Gramene; KJB81519; KJB81519; B456_013G150100.
DR Gramene; KJB81522; KJB81522; B456_013G150100.
DR Gramene; KJB81523; KJB81523; B456_013G150100.
DR Gramene; KJB81524; KJB81524; B456_013G150100.
DR KEGG; gra:105783095; -.
DR eggNOG; KOG4203; Eukaryota.
DR OMA; YHIVDSH; -.
DR OrthoDB; 180154at2759; -.
DR UniPathway; UPA00574; UER00637.
DR UniPathway; UPA00579; UER00640.
DR Proteomes; UP000032304; Chromosome 13.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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; 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:UP000032304};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003825}.
FT DOMAIN 49..235
FT /note="Phosphoribulokinase/uridine kinase"
FT /evidence="ECO:0000259|Pfam:PF00485"
SQ SEQUENCE 479 AA; 53867 MW; B68DE3FD674D5406 CRC64;
MDSKSVEDMI EGLSGFHFSG FHMDGSKLNN IEKPTTTLAI ENVHKQPFII GVAGGAASGK
TTVCDMIIQQ LHDQRVVLVN QDSFYHKLTE EELATVHEYN FDHPDSFDTE KLLDSMENLR
HGQAVDIPNY DFKSYKNSVF PARRVNPADV IILEGILIFH DPRVRELMNM KIFVDTDADV
RLARRIRRDT VEKGRDIGVV LDQYSKFVKS AFDDFILPTK KYADIIIPRG GDNHVAIDLI
VQHIRTKLGQ HDLCKIYPNL YVIQSTFQIR GMHTLIRDSQ TTKHDFVFYA DRLIRLVVEH
GLGHLPFTEK QVITPTGSVY TGVDFCKRLC GVSVIRSGES MENALRACCK GIKIGKILIH
REGEDNGQQL IYEKLPQDIS ERHVLLLDPI LGTGNTAVKA ISLLTRKGVP ESNIIFLNLI
SAPQGVHVVC KSFPRVKIVT SEIDIGLNEG FRVIPGMGEF GDRYFGTDDD DLQVVPPSQ
//
