ID G1W8N3_9BACT Unreviewed; 209 AA.
AC G1W8N3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
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=HMPREF9431_00184 {ECO:0000313|EMBL:EGV34620.1};
OS Segatella oulorum F0390.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Segatella.
OX NCBI_TaxID=702438 {ECO:0000313|EMBL:EGV34620.1, ECO:0000313|Proteomes:UP000005141};
RN [1] {ECO:0000313|EMBL:EGV34620.1, ECO:0000313|Proteomes:UP000005141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0390 {ECO:0000313|EMBL:EGV34620.1,
RC ECO:0000313|Proteomes:UP000005141};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A.,
RA Baranova O.V., Blanton J.M., Tanner A.C., Dewhirst F.E., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Prevotella oulorum F0390.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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: 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:EGV34620.1}.
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DR EMBL; ADGI01000012; EGV34620.1; -; Genomic_DNA.
DR RefSeq; WP_004379157.1; NZ_JH114215.1.
DR AlphaFoldDB; G1W8N3; -.
DR PATRIC; fig|702438.4.peg.188; -.
DR eggNOG; COG0572; Bacteria.
DR HOGENOM; CLU_021278_1_2_10; -.
DR OrthoDB; 9777642at2; -.
DR UniPathway; UPA00574; UER00637.
DR UniPathway; UPA00579; UER00640.
DR Proteomes; UP000005141; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR003593; AAA+_ATPase.
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 SMART; SM00382; AAA; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000005141};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00551}.
FT DOMAIN 5..163
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 13..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00551"
SQ SEQUENCE 209 AA; 24027 MW; 90FD9BFD23529FFA CRC64;
MFEDKTTIIG IAGGTGSGKT TVVKKIVEAL PPHYVAVVPL DSYYNDTSHM TDEERHAINF
DHPDAFDWKL LHKQVNDLRE GRAIEQPTYS YLQCNRLSET IHVEPKPVII IEGIMTLLNK
KLRDLMDLKI FVDCDPDERL IRNIQRDTID RGRTVSMVVE RYLEVLKPMH EQFIEPTKRF
ADIIIPQGGE NTRGISILRN YIEGLVPKE
//
