ID A6VMP4_ACTSZ Unreviewed; 212 AA.
AC A6VMP4;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 110.
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 OrderedLocusNames=Asuc_0871 {ECO:0000313|EMBL:ABR74241.1};
OS Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS 130Z).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=339671 {ECO:0000313|EMBL:ABR74241.1, ECO:0000313|Proteomes:UP000001114};
RN [1] {ECO:0000313|Proteomes:UP000001114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z
RC {ECO:0000313|Proteomes:UP000001114};
RX PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA Burkhart K.B., Harkins V., Vieille C.;
RT "A genomic perspective on the potential of Actinobacillus succinogenes for
RT industrial succinate production.";
RL BMC Genomics 11:680-680(2010).
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; CP000746; ABR74241.1; -; Genomic_DNA.
DR AlphaFoldDB; A6VMP4; -.
DR STRING; 339671.Asuc_0871; -.
DR KEGG; asu:Asuc_0871; -.
DR eggNOG; COG0572; Bacteria.
DR HOGENOM; CLU_021278_1_2_6; -.
DR OrthoDB; 9777642at2; -.
DR UniPathway; UPA00574; UER00637.
DR UniPathway; UPA00579; UER00640.
DR Proteomes; UP000001114; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000001114};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00551}.
FT DOMAIN 8..197
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 212 AA; 24123 MW; 61578A78FE5445A4 CRC64;
MAEISCIIIG IAGASASGKS LIASTVHDEL LRELGCGDIG IITEDSYYKD QSHLDFETRT
KTNYDHPNSM DRDLLIEHLR ALKAGNAVDI PVYNYAEHNR SAEITRFEPR KIIILEGILL
LTDERVRNEL SMSVFVDTPL DICFIRRLQR DMVQRGRSME SVIQQYRTTV RPMFMQFIEP
SKQYADVIIP RGGKNRVAIE LLKAQILKLL GK
//
