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Entry: T0CSV5_ALIAG
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Original site: T0CSV5_ALIAG 
ID   T0CSV5_ALIAG            Unreviewed;       205 AA.
AC   T0CSV5; A0A9E7CR92;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 59.
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   ECO:0000313|EMBL:UNO49464.1};
GN   ORFNames=K1I37_02625 {ECO:0000313|EMBL:UNO49464.1};
OS   Alicyclobacillus acidoterrestris (strain ATCC 49025 / DSM 3922 / CIP 106132
OS   / NCIMB 13137 / GD3B).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Alicyclobacillus.
OX   NCBI_TaxID=1356854 {ECO:0000313|EMBL:UNO49464.1, ECO:0000313|Proteomes:UP000829401};
RN   [1] {ECO:0000313|Proteomes:UP000829401}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3922 {ECO:0000313|Proteomes:UP000829401};
RX   PubMed=36240455; DOI=10.1093/g3journal/jkac225;
RA   Leonardo I.C., Barreto Crespo M.T., Gaspar F.B.;
RT   "Unveiling the complete genome sequence of Alicyclobacillus acidoterrestris
RT   DSM 3922T, a taint-producing strain.";
RL   G3 (Bethesda) 12:0-0(2022).
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}.
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DR   EMBL; CP080467; UNO49464.1; -; Genomic_DNA.
DR   RefSeq; WP_021298130.1; NZ_AURB01000175.1.
DR   STRING; 1356854.N007_01710; -.
DR   KEGG; aaco:K1I37_02625; -.
DR   Proteomes; UP000829401; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0008655; P:pyrimidine-containing compound salvage; IEA:UniProtKB-UniRule.
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}; Reference proteome {ECO:0000313|Proteomes:UP000829401};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00551}.
FT   DOMAIN          3..189
FT                   /note="Phosphoribulokinase/uridine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00485"
FT   BINDING         8..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00551"
SQ   SEQUENCE   205 AA;  23129 MW;  0BDDAA8CF6EE4D34 CRC64;
     MLIIGIAGGT GSGKTSVARA ILEQLGAQSV ALISQDAYYQ DHSDLPFERR QQLNYDHPDS
     FDNDLLREHV TTLRQGGSIE MPIYDFKTHN RSAQTIHVPA RPVIILEGIH VLVDPELRAL
     LDIKVFVDTD PDVRVLRRIR RDIEERGRSI ESVYDQYLST VKPMHDAFIE PSKRFADLII
     PEGGQNQIAI ALLTTRVSQF LSENN
//
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