ID A0A0R1M1Y2_9LACO Unreviewed; 219 AA.
AC A0A0R1M1Y2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Uridine kinase {ECO:0000256|ARBA:ARBA00021478, ECO:0000256|HAMAP-Rule:MF_00551};
DE EC=2.7.1.48 {ECO:0000256|ARBA:ARBA00012137, ECO:0000256|HAMAP-Rule:MF_00551};
DE AltName: Full=Cytidine monophosphokinase {ECO:0000256|HAMAP-Rule:MF_00551};
DE AltName: Full=Uridine monophosphokinase {ECO:0000256|HAMAP-Rule:MF_00551};
GN Name=udk {ECO:0000256|HAMAP-Rule:MF_00551};
GN ORFNames=FD04_GL000918 {ECO:0000313|EMBL:KRK97943.1};
OS Secundilactobacillus odoratitofui DSM 19909 = JCM 15043.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Secundilactobacillus.
OX NCBI_TaxID=1423776 {ECO:0000313|EMBL:KRK97943.1, ECO:0000313|Proteomes:UP000051160};
RN [1] {ECO:0000313|EMBL:KRK97943.1, ECO:0000313|Proteomes:UP000051160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19909 {ECO:0000313|EMBL:KRK97943.1,
RC ECO:0000313|Proteomes:UP000051160};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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, ECO:0000256|HAMAP-
CC Rule:MF_00551, ECO:0000256|RuleBase:RU003825};
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway;
CC CTP from cytidine: step 1/3. {ECO:0000256|ARBA:ARBA00004784,
CC ECO:0000256|HAMAP-Rule:MF_00551, 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|HAMAP-Rule:MF_00551, ECO:0000256|RuleBase:RU003825}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00551,
CC ECO:0000256|RuleBase:RU003825}.
CC -!- SIMILARITY: Belongs to the uridine kinase family.
CC {ECO:0000256|ARBA:ARBA00005408, ECO:0000256|HAMAP-Rule:MF_00551,
CC ECO:0000256|RuleBase:RU003825}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00551}.
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:KRK97943.1}.
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DR EMBL; AZEE01000028; KRK97943.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1M1Y2; -.
DR STRING; 1423776.FD04_GL000918; -.
DR PATRIC; fig|1423776.4.peg.925; -.
DR UniPathway; UPA00574; UER00637.
DR UniPathway; UPA00579; UER00640.
DR Proteomes; UP000051160; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043771; F:cytidine kinase activity; IEA:RHEA.
DR GO; GO:0004849; F:uridine kinase activity; IEA:UniProtKB-UniRule.
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 HAMAP; MF_00551; Uridine_kinase; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006083; PRK/URK.
DR InterPro; IPR026008; Uridine_kinase.
DR InterPro; IPR000764; Uridine_kinase-like.
DR NCBIfam; TIGR00235; udk; 1.
DR PANTHER; PTHR10285; URIDINE KINASE; 1.
DR PANTHER; PTHR10285:SF226; URIDINE KINASE; 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|HAMAP-Rule:MF_00551,
KW ECO:0000256|RuleBase:RU003825};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00551, ECO:0000256|RuleBase:RU003825};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00551};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00551};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00551}.
FT DOMAIN 12..198
FT /note="Phosphoribulokinase/uridine kinase"
FT /evidence="ECO:0000259|Pfam:PF00485"
SQ SEQUENCE 219 AA; 25290 MW; CA1CF49A5C96B09A CRC64;
MFKMSAQSKP VIIGVTGGSS SGKTTVSRAI YDELANESIM ILQQDAYYND QAEMSMAERK
AVNYDHPLAF DTDLLVQQLQ QLRQNQSIEV PVYDYTKYTR SPETVHQDPK DVIIVEGILI
LDDERLRDLM DIKVFVDTDD DIRIIRRIER DIKERQRDLD GIIDQYLTTV KPMYHQFVEP
TKRYADLIVP EGGENQVAID LLTTKIRSIL LQKKNGRHE
//
