ID F2NL98_MARHT Unreviewed; 205 AA.
AC F2NL98;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 28-MAR-2018, entry version 49.
DE RecName: Full=Uridine kinase {ECO:0000256|HAMAP-Rule:MF_00551, ECO:0000256|RuleBase:RU003825, ECO:0000256|SAAS:SAAS00847169};
DE EC=2.7.1.48 {ECO:0000256|HAMAP-Rule:MF_00551, ECO:0000256|RuleBase:RU003825, ECO:0000256|SAAS:SAAS00852590};
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 OrderedLocusNames=Marky_0973 {ECO:0000313|EMBL:AEB11717.1};
OS Marinithermus hydrothermalis (strain DSM 14884 / JCM 11576 / T1).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC Marinithermus.
OX NCBI_TaxID=869210 {ECO:0000313|EMBL:AEB11717.1, ECO:0000313|Proteomes:UP000007030};
RN [1] {ECO:0000313|EMBL:AEB11717.1, ECO:0000313|Proteomes:UP000007030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14884 / JCM 11576 / T1 {ECO:0000313|Proteomes:UP000007030};
RX PubMed=22675595; DOI=10.4056/sigs.2435521;
RA Copeland A., Gu W., Yasawong M., Lapidus A., Lucas S., Deshpande S.,
RA Pagani I., Tapia R., Cheng J.F., Goodwin L.A., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Pan C., Brambilla E.M., Rohde M.,
RA Tindall B.J., Sikorski J., Goker M., Detter J.C., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Woyke T.;
RT "Complete genome sequence of the aerobic, heterotroph Marinithermus
RT hydrothermalis type strain (T1(T)) from a deep-sea hydrothermal vent
RT chimney.";
RL Stand. Genomic Sci. 6:21-30(2012).
CC -!- CATALYTIC ACTIVITY: ATP + cytidine = ADP + CMP.
CC {ECO:0000256|HAMAP-Rule:MF_00551, ECO:0000256|RuleBase:RU003825,
CC ECO:0000256|SAAS:SAAS00852610}.
CC -!- CATALYTIC ACTIVITY: ATP + uridine = ADP + UMP. {ECO:0000256|HAMAP-
CC Rule:MF_00551, ECO:0000256|RuleBase:RU003825,
CC ECO:0000256|SAAS:SAAS00852616}.
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage
CC pathway; CTP from cytidine: step 1/3. {ECO:0000256|HAMAP-
CC Rule:MF_00551, ECO:0000256|RuleBase:RU003825,
CC ECO:0000256|SAAS:SAAS00852620}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage
CC pathway; UMP from uridine: step 1/1. {ECO:0000256|HAMAP-
CC Rule:MF_00551, ECO:0000256|RuleBase:RU003825,
CC ECO:0000256|SAAS:SAAS00852602}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00551,
CC ECO:0000256|RuleBase:RU003825, ECO:0000256|SAAS:SAAS00847170}.
CC -!- SIMILARITY: Belongs to the uridine kinase family.
CC {ECO:0000256|HAMAP-Rule:MF_00551, ECO:0000256|RuleBase:RU003825,
CC ECO:0000256|SAAS:SAAS00852607}.
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DR EMBL; CP002630; AEB11717.1; -; Genomic_DNA.
DR RefSeq; WP_013703765.1; NC_015387.1.
DR STRING; 869210.Marky_0973; -.
DR EnsemblBacteria; AEB11717; AEB11717; Marky_0973.
DR KEGG; mhd:Marky_0973; -.
DR eggNOG; ENOG4105DBI; Bacteria.
DR eggNOG; COG0572; LUCA.
DR KO; K00876; -.
DR OMA; TTLKPMH; -.
DR OrthoDB; POG091H04CS; -.
DR BioCyc; MHYD869210:G1GSR-987-MONOMER; -.
DR UniPathway; UPA00574; UER00637.
DR UniPathway; UPA00579; UER00640.
DR Proteomes; UP000007030; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR GO; GO:0004849; F:uridine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0044211; P:CTP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR CDD; cd02023; UMPK; 1.
DR HAMAP; MF_00551; Uridine_kinase; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006083; PRK/URK.
DR InterPro; IPR000764; Uridine_kinase-like.
DR InterPro; IPR026008; Uridine_kinase_.
DR Pfam; PF00485; PRK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00235; udk; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00551,
KW ECO:0000256|RuleBase:RU003825, ECO:0000256|SAAS:SAAS00852588};
KW Complete proteome {ECO:0000313|Proteomes:UP000007030};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00551,
KW ECO:0000256|RuleBase:RU003825, ECO:0000256|SAAS:SAAS00847174};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00551,
KW ECO:0000256|RuleBase:RU003825, ECO:0000256|SAAS:SAAS00852585,
KW ECO:0000313|EMBL:AEB11717.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00551,
KW ECO:0000256|RuleBase:RU003825, ECO:0000256|SAAS:SAAS00852604};
KW Reference proteome {ECO:0000313|Proteomes:UP000007030};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00551,
KW ECO:0000256|RuleBase:RU003825, ECO:0000256|SAAS:SAAS00852593}.
FT DOMAIN 5 188 PRK. {ECO:0000259|Pfam:PF00485}.
FT NP_BIND 10 17 ATP. {ECO:0000256|HAMAP-Rule:MF_00551}.
SQ SEQUENCE 205 AA; 23475 MW; DECDC375521332AC CRC64;
MKPFVIGIAG GTGSGKTTVT ERVIETVGRD RVALVPMDNY YKDQSHLPFE ERTRINYDHP
AAFDTGLLLE HLEALMNGVP IEMPLYSFTE HVRLLETATV APAPVVVIEG ILALYDEHLR
RLMDLKVFVD ADPDVRFIRR LERDIRERGR TLESVIRQYL EFVRPMHLSF VEPTKRYADV
IIPRGGHNQP ALEMLVSRIR TLIEV
//
