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Database: UniProt
Entry: A0A239ZS54_CLOCO
LinkDB: A0A239ZS54_CLOCO
Original site: A0A239ZS54_CLOCO 
ID   A0A239ZS54_CLOCO        Unreviewed;       210 AA.
AC   A0A239ZS54;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
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_1 {ECO:0000313|EMBL:SQB33936.1};
GN   Synonyms=udk {ECO:0000256|HAMAP-Rule:MF_00551,
GN   ECO:0000313|EMBL:NOH16527.1};
GN   ORFNames=HMJ28_09030 {ECO:0000313|EMBL:NOH16527.1}, NCTC13028_00814
GN   {ECO:0000313|EMBL:SQB33936.1}, SAMN05216497_10123
GN   {ECO:0000313|EMBL:SDK80478.1};
OS   Clostridium cochlearium.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1494 {ECO:0000313|EMBL:SQB33936.1, ECO:0000313|Proteomes:UP000250223};
RN   [1] {ECO:0000313|EMBL:SDK80478.1, ECO:0000313|Proteomes:UP000198811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NLAE-zl-C224 {ECO:0000313|EMBL:SDK80478.1,
RC   ECO:0000313|Proteomes:UP000198811};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SQB33936.1, ECO:0000313|Proteomes:UP000250223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC13028 {ECO:0000313|EMBL:SQB33936.1,
RC   ECO:0000313|Proteomes:UP000250223};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:NOH16527.1, ECO:0000313|Proteomes:UP000528432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AGROS13 {ECO:0000313|EMBL:NOH16527.1,
RC   ECO:0000313|Proteomes:UP000528432};
RA   Gupta T.B., Jauregui R., Risson A.N., Brightwell G., Maclean P.;
RT   "Draft genome sequence of Clostridium cochlearium strain AGROS13 isolated
RT   from a sheep dairy farm in New Zealand.";
RL   Submitted (MAY-2020) 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}.
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DR   EMBL; JABFIF010000018; NOH16527.1; -; Genomic_DNA.
DR   EMBL; FNGL01000001; SDK80478.1; -; Genomic_DNA.
DR   EMBL; UAWC01000003; SQB33936.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239ZS54; -.
DR   STRING; 1494.SAMN05216497_10123; -.
DR   OrthoDB; 9777642at2; -.
DR   UniPathway; UPA00574; UER00637.
DR   UniPathway; UPA00579; UER00640.
DR   Proteomes; UP000198811; Unassembled WGS sequence.
DR   Proteomes; UP000250223; Unassembled WGS sequence.
DR   Proteomes; UP000528432; 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: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: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          8..194
FT                   /note="Phosphoribulokinase/uridine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00485"
FT   BINDING         13..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00551"
SQ   SEQUENCE   210 AA;  24543 MW;  4951F25E7F010C1D CRC64;
     MSKRRPMLIG ITGGTGSGKS TVSKEICRKF DKDLIVMIEQ DSYYRDQSHL SIEERVKTNY
     DHPNAFDTEL LVEHLRELSN WNKIEKPIYD FELHNRKKET EIVEPTEIII VEGILVLEEK
     EIRDLLDIKI YVDTDADVRI IRRLVRDIKE RGRTLDSVIN QYLNVVRPMH MQFIEPSKRY
     ADIIIPEGGH NKVAIDIIVG NIKQMLQKSE
//
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