ID A0A1V9ZXG6_9STRA Unreviewed; 1938 AA.
AC A0A1V9ZXG6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Uridine kinase {ECO:0000256|RuleBase:RU003825};
DE EC=2.7.1.48 {ECO:0000256|RuleBase:RU003825};
GN ORFNames=THRCLA_04990 {ECO:0000313|EMBL:OQS02641.1};
OS Thraustotheca clavata.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Thraustotheca.
OX NCBI_TaxID=74557 {ECO:0000313|EMBL:OQS02641.1, ECO:0000313|Proteomes:UP000243217};
RN [1] {ECO:0000313|EMBL:OQS02641.1, ECO:0000313|Proteomes:UP000243217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQS02641.1,
RC ECO:0000313|Proteomes:UP000243217};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
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:OQS02641.1}.
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DR EMBL; JNBS01001098; OQS02641.1; -; Genomic_DNA.
DR STRING; 74557.A0A1V9ZXG6; -.
DR OrthoDB; 46768at2759; -.
DR UniPathway; UPA00574; UER00637.
DR UniPathway; UPA00579; UER00640.
DR Proteomes; UP000243217; 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006083; PRK/URK.
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|RuleBase:RU003825};
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000243217};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003825}.
FT DOMAIN 1752..1932
FT /note="Phosphoribulokinase/uridine kinase"
FT /evidence="ECO:0000259|Pfam:PF00485"
FT COILED 578..629
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1938 AA; 225224 MW; 50B48C11DB314211 CRC64;
MIDHSSNSSL SCKKRKFDPI ERIKPSKDPR LAHIRSKRIR QLESLMHYVY DLESEISRIK
RERATLLPLP WEDVAGALKD DTLEQVRLNR SLKCQVEAYS HLTAVLQSWI TSMNPETRIP
SQYEETWQHS QLMAADPIVR KVGATWILQQ VYNNTMRVMA KANFPSTLTS SMDIQVDNRM
DTKSIPKRER ARKKFAAPAR IRPSKDPRLA HIRSKRARQM QSMRNYLYDL TDRLTILHNR
HHQPSMLSWH DILKALQDDT LEQVRENRAL KQQIDHAERL KTMLEDWVTR IIQPNQRVPS
ITEETWRHSQ LLAGDEASRQ IAFEWILRQV YHNTTRALAH VHYPDTATSC ITIDISLLEN
EDKPILLVQG MTQDIMPYPL EEVINGYWVT EKTFAQAFRH QNTPITLQSC DIENANQEMQ
YLREEVPYPD GRIVHYNVLT GRFLEQDRMT IALRTILKDS AFPDMPENNM QWIVDTKQWI
VADRINSNST RCRTFYTIRH PFTPMGDVSL HDLASSYGVN AATDSEILVL LKRQLSIGHY
EQRSFGGTVN CVLRNNIDMS TKRAPRRRKP ESRYTYQLDA LKREIYDMEC IIQRLKRQRN
SALSWEDIAK ALQDDMLRLV KENRNLQHSR QAYTRFYHVL HACAQLHIDR APTLAEETWR
HGQLLSGDVS TRHLGYEWIL KQVQYNTPRA MSYARFPNSL ENYVDVQVTT TDNLINIHVT
TQQVVAFSLQ EVTSAYWIAE QSFARMYMGQ TIEVEDELLL QQAQSVLENI QYVQEILDYG
PFNVCYNVLS GQFTEETRTT LVLRTILQDE AHPTSPNSWI VDTKQWTVAD QLCPNMTRCR
TYYTIQHPIR SSDQCSLSLH DFALMFQLPT NDPTNLVSIL KARSEANHLR QRTYFQTYFE
SVLTTLRRHL TKRVLALFTM TTKKQRMTIK LPIKPSKDPR FDHIKSRRAK SLEALRRYVF
ELEEQVAKLK RGKVALLPWE DIALALKDDM LEMVRDNRSL KRDVEYRKRM CRFLQECFFR
PNPLGMAPSV AEETWQHSQL LAGDVSSRKT GCEWILQQLY HNTERAMAHI QFPENNQLDV
IDINVACSNE NLITVEVMSQ EYLPYSLEHV AEAYGFAAAS FSKAYMRKVA GYLDDTKTGL
TDEAFHYESV QLQDHHTTIR YNTLSRFFQS GDRCILALRT ILKDEAYPVA GTTWIMNTKQ
WVVIDKLEPK LTRCRTFYTI DHPFSEAGGY VPVADLTRNR GLPVGTDDTQ NVRMLRDRYY
EQHWLQRSFF QMHARCVADT IASKYDEDWD TIMDDPDQSS WLLIVCFYVG QEAIELPQLA
NIKSKRVKEL EYLRRQVYIL QGHIEKIRRC QSTLLSWEDV AHALKDDTLD QVRDNRSLKK
KLHQNKCVGR FLKHWMYSTT PCRPPSITEE YWRYSLLVAG DEAARQIGYE WIARQAYHNT
QAAMTHVSFD NNQTDYVQVQ VNISGENHFF VQVLAQQFVD FDLDAVHDAF WIAEKSFAAS
FRKKSTDLKD LSLPNKDIVY LCENLGTSTQ RIFNKTIQAR FREADSSTFI LRSILKDEMF
PDDNIEDAWS FNTKFWMVAN GMPDGRTRCR TFYTLDHPLT EKNGFVSLPE LARCVGLVMP
NESHLVNVVK ERFLNSHHAQ RLFFAQHLRN IKFKVSFVLT NQIEVYETRQ VIEMSAQSRH
LLPVVVLGCL AVAAFVYMKQ RKTGSAKPPL IPRKPTNARV SSDLTDTQMV YTEPEGVKIT
RRGSVGPNDI LVIGVCGGTG SGKTTLSRAI IDEIGEANVS YLSHDYYYRD ISHKTLEQRA
QHNFDHPDSL ETSLLVRHLQ HLRDGETVEV PVYDFTTHSR CSHTQTMVPR RVILVEGILL
FTDPDLVALM DIKVFVETPS DIRFIRRLRR DIADRGRTAE GVIEQYLKTV RPMHLTFVEP
SKRVADIIVP VGVNALSK
//
