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Database: UniProt
Entry: A0A367XVA5_9ASCO
LinkDB: A0A367XVA5_9ASCO
Original site: A0A367XVA5_9ASCO 
ID   A0A367XVA5_9ASCO        Unreviewed;       545 AA.
AC   A0A367XVA5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   13-SEP-2023, entry version 20.
DE   RecName: Full=Uridine kinase {ECO:0000256|RuleBase:RU003825};
DE            EC=2.7.1.48 {ECO:0000256|RuleBase:RU003825};
GN   Name=URK1_1 {ECO:0000313|EMBL:RCK57339.1};
GN   ORFNames=Cantr_06359 {ECO:0000313|EMBL:RCK57339.1};
OS   Candida viswanathii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5486 {ECO:0000313|EMBL:RCK57339.1, ECO:0000313|Proteomes:UP000253472};
RN   [1] {ECO:0000313|EMBL:RCK57339.1, ECO:0000313|Proteomes:UP000253472}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20962 {ECO:0000313|EMBL:RCK57339.1,
RC   ECO:0000313|Proteomes:UP000253472};
RA   Ahn J.;
RT   "Whole genome sequencing of Candida tropicalis (genome annotated by CSBL at
RT   Korea University).";
RL   Submitted (JUN-2018) 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|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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RCK57339.1}.
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DR   EMBL; QLNQ01000028; RCK57339.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367XVA5; -.
DR   STRING; 5486.A0A367XVA5; -.
DR   UniPathway; UPA00574; UER00637.
DR   UniPathway; UPA00579; UER00640.
DR   Proteomes; UP000253472; Unassembled WGS sequence.
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; 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; 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:UP000253472};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003825}.
FT   DOMAIN          96..283
FT                   /note="Phosphoribulokinase/uridine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00485"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          52..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   545 AA;  61432 MW;  47C7675AA358536C CRC64;
     MPLNPKPRRR SSRISPIADE ESLSFINSSV ENLDPSPFES IDDLVDDMNN LSSADRRSSF
     TPTIPSGAGT PTTASATGGT TTPKASYIPP WTEPYIIGIA GNSGSGKTSI SQQIIQEINQ
     PWTVLLSFDN FYNPLTPEES KRAFANNFDF DTPDSLDFEL LVETIKNLKR GGKATIPVYS
     FTSHNRTNKT NTIYGANVII VEGLYALYDE RLLDMMDLKI YVDTDLDICL ARRLTRDILY
     RGRDLGGAIQ QWERFVKPNA VKFINPTMHN ADLVIPRGLD NSIAINLMIN HINNQLANKS
     RNHISRLRKL GININFDVNQ FNIKLLRDTN QVRGINSILF DTETSRNDFI FYFNRICGLL
     IELAQEFITD YQEVDIETGK GIYHGKQVVQ NQYIAINIIR SGDCFMSSIK RSFPEISIGK
     LLIQSDSSTG EPQLHFESLP LNLTEKGEIM LFDSQIISGA GAIMAIQVLL DHGVKESDII
     LISYLSTEIG VRRIVNVFPK VKIVIGKLSN MEDLSTKSWY NQEGFLDSHW HFRNRFIDSL
     YFGTD
//
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