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URK_THET8
ID   URK_THET8               Reviewed;         211 AA.
AC   Q5SKR5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Uridine kinase {ECO:0000255|HAMAP-Rule:MF_00551};
DE            EC=2.7.1.48 {ECO:0000255|HAMAP-Rule:MF_00551};
DE   AltName: Full=Cytidine monophosphokinase {ECO:0000255|HAMAP-Rule:MF_00551};
DE   AltName: Full=Uridine monophosphokinase {ECO:0000255|HAMAP-Rule:MF_00551};
GN   Name=udk {ECO:0000255|HAMAP-Rule:MF_00551}; OrderedLocusNames=TTHA0578;
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-Rule:MF_00551};
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:0000255|HAMAP-Rule:MF_00551};
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway;
CC       CTP from cytidine: step 1/3. {ECO:0000255|HAMAP-Rule:MF_00551}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC       UMP from uridine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00551}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00551}.
CC   -!- SIMILARITY: Belongs to the uridine kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00551}.
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DR   EMBL; AP008226; BAD70401.1; -; Genomic_DNA.
DR   RefSeq; WP_011172663.1; NC_006461.1.
DR   RefSeq; YP_143844.1; NC_006461.1.
DR   PDB; 3ASY; X-ray; 2.40 A; A/B=1-211.
DR   PDB; 3ASZ; X-ray; 2.25 A; A/B=1-211.
DR   PDB; 3W34; X-ray; 1.91 A; A/B=1-211.
DR   PDB; 3W8R; X-ray; 2.50 A; A/B=1-211.
DR   PDBsum; 3ASY; -.
DR   PDBsum; 3ASZ; -.
DR   PDBsum; 3W34; -.
DR   PDBsum; 3W8R; -.
DR   AlphaFoldDB; Q5SKR5; -.
DR   SMR; Q5SKR5; -.
DR   STRING; 300852.55771960; -.
DR   EnsemblBacteria; BAD70401; BAD70401; BAD70401.
DR   GeneID; 3168643; -.
DR   KEGG; ttj:TTHA0578; -.
DR   PATRIC; fig|300852.9.peg.577; -.
DR   eggNOG; COG0572; Bacteria.
DR   HOGENOM; CLU_021278_1_2_0; -.
DR   OMA; TTLKPMH; -.
DR   PhylomeDB; Q5SKR5; -.
DR   BRENDA; 2.7.1.48; 2305.
DR   UniPathway; UPA00574; UER00637.
DR   UniPathway; UPA00579; UER00640.
DR   EvolutionaryTrace; Q5SKR5; -.
DR   Proteomes; UP000000532; Chromosome.
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; -; 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   Pfam; PF00485; PRK; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00235; udk; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..211
FT                   /note="Uridine kinase"
FT                   /id="PRO_1000081978"
FT   BINDING         13..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00551"
FT   STRAND          7..14
FT                   /evidence="ECO:0007829|PDB:3W34"
FT   HELIX           19..30
FT                   /evidence="ECO:0007829|PDB:3W34"
FT   HELIX           31..33
FT                   /evidence="ECO:0007829|PDB:3W34"
FT   STRAND          34..38
FT                   /evidence="ECO:0007829|PDB:3W34"
FT   HELIX           39..41
FT                   /evidence="ECO:0007829|PDB:3W34"
FT   HELIX           51..56
FT                   /evidence="ECO:0007829|PDB:3W34"
FT   HELIX           62..64
FT                   /evidence="ECO:0007829|PDB:3W34"
FT   HELIX           67..78
FT                   /evidence="ECO:0007829|PDB:3W34"
FT   STRAND          83..89
FT                   /evidence="ECO:0007829|PDB:3W34"
FT   TURN            90..93
FT                   /evidence="ECO:0007829|PDB:3W34"
FT   STRAND          94..102
FT                   /evidence="ECO:0007829|PDB:3W34"
FT   STRAND          106..112
FT                   /evidence="ECO:0007829|PDB:3W34"
FT   TURN            113..116
FT                   /evidence="ECO:0007829|PDB:3W34"
FT   HELIX           119..122
FT                   /evidence="ECO:0007829|PDB:3W34"
FT   STRAND          126..132
FT                   /evidence="ECO:0007829|PDB:3W34"
FT   HELIX           135..149
FT                   /evidence="ECO:0007829|PDB:3W34"
FT   HELIX           154..163
FT                   /evidence="ECO:0007829|PDB:3W34"
FT   HELIX           165..171
FT                   /evidence="ECO:0007829|PDB:3W34"
FT   HELIX           174..179
FT                   /evidence="ECO:0007829|PDB:3W34"
FT   STRAND          181..186
FT                   /evidence="ECO:0007829|PDB:3W34"
FT   HELIX           191..209
FT                   /evidence="ECO:0007829|PDB:3W34"
SQ   SEQUENCE   211 AA;  23674 MW;  8A64A64FF033E6B0 CRC64;
     MSAPKPFVIG IAGGTASGKT TLAQALARTL GERVALLPMD HYYKDLGHLP LEERLRVNYD
     HPDAFDLALY LEHAQALLRG LPVEMPVYDF RAYTRSPRRT PVRPAPVVIL EGILVLYPKE
     LRDLMDLKVF VDADADERFI RRLKRDVLER GRSLEGVVAQ YLEQVKPMHL HFVEPTKRYA
     DVIVPRGGQN PVALEMLAAK ALARLARMGA A
 
 
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