ID C5DVS4_ZYGRC Unreviewed; 487 AA.
AC C5DVS4;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 13-SEP-2023, entry version 82.
DE RecName: Full=Uridine kinase {ECO:0000256|RuleBase:RU003825};
DE EC=2.7.1.48 {ECO:0000256|RuleBase:RU003825};
GN OrderedLocusNames=ZYRO0D09020g {ECO:0000313|EMBL:CAR27893.1};
OS Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS / NRRL Y-229) (Candida mogii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX NCBI_TaxID=559307 {ECO:0000313|EMBL:CAR27893.1, ECO:0000313|Proteomes:UP000008536};
RN [1] {ECO:0000313|Proteomes:UP000008536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC Y-229 {ECO:0000313|Proteomes:UP000008536};
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
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|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|RuleBase:RU003825};
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway;
CC CTP from cytidine: step 1/3. {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|RuleBase:RU003825}.
CC -!- SIMILARITY: Belongs to the uridine kinase family.
CC {ECO:0000256|RuleBase:RU003825}.
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DR EMBL; CU928176; CAR27893.1; -; Genomic_DNA.
DR RefSeq; XP_002496826.1; XM_002496781.1.
DR AlphaFoldDB; C5DVS4; -.
DR STRING; 559307.C5DVS4; -.
DR GeneID; 8204083; -.
DR KEGG; zro:ZYRO0D09020g; -.
DR HOGENOM; CLU_021278_0_2_1; -.
DR InParanoid; C5DVS4; -.
DR UniPathway; UPA00574; UER00637.
DR UniPathway; UPA00579; UER00640.
DR Proteomes; UP000008536; Chromosome D.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043771; F:cytidine kinase activity; IEA:RHEA.
DR GO; GO:0004849; F:uridine kinase activity; IEA:UniProtKB-EC.
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; cd06223; PRTases_typeI; 1.
DR CDD; cd02023; UMPK; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR006083; PRK/URK.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR000764; Uridine_kinase-like.
DR NCBIfam; TIGR00235; udk; 1.
DR PANTHER; PTHR10285; URIDINE KINASE; 1.
DR PANTHER; PTHR10285:SF215; URIDINE KINASE; 1.
DR Pfam; PF00485; PRK; 1.
DR Pfam; PF14681; UPRTase; 1.
DR PRINTS; PR00988; URIDINKINASE.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003825};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003825};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003825};
KW Reference proteome {ECO:0000313|Proteomes:UP000008536};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003825}.
FT DOMAIN 46..234
FT /note="Phosphoribulokinase/uridine kinase"
FT /evidence="ECO:0000259|Pfam:PF00485"
SQ SEQUENCE 487 AA; 54884 MW; 361A898C7996CA52 CRC64;
MTASNTPSPT ILESTNVAKV HHSDANGHHS KSKRFQYLPP WTTPYVIGVG GPSGSGKTSV
AAKIVSSLNV PWTVLISLDN FYKPLNAEQR RTAFENNYDF DHPTALDLDL AYEAISSLKE
GKKTTIPVYS FVEHNRIPNK NITIYGASII VLEGIYTLYD KRLLDLMDLK IYVDADLDVC
LARRLSRDIV YRGRDLEGCL EQWERFVKPN AERYLRPKMK EADAIVPSLT DNGVAVELII
NHIKSRLQQK SEEHLKELIE LGHSDLVNVS EHPSLHELVP TNQVNAIITM LLNKMTSRYD
FVFYFDRIAT ILLTQVLSDI PVYEKCTIET PEGTTIPDAL KCDFNQITAI NLIESGDCFM
HSLKKTIPNI VTGKLLVQSD SRTGEPQLHF KLLPPDITNY KMVLLTEAQM ISGASMIMST
QVLLDHGVEL ENIKVVVFLA TEISIRRILN AFDGKVDIYV GKIVTKNELN RCDWAKARFV
GAKYFGW
//
