(data stored in ACNUC10043 zone)

SWISSPROT: D1YVH5_METPS

ID   D1YVH5_METPS            Unreviewed;       223 AA.
AC   D1YVH5;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   11-DEC-2019, entry version 68.
DE   RecName: Full=Uridylate kinase {ECO:0000256|HAMAP-Rule:MF_01220};
DE            Short=UK {ECO:0000256|HAMAP-Rule:MF_01220};
DE            EC=2.7.4.22 {ECO:0000256|HAMAP-Rule:MF_01220};
DE   AltName: Full=Uridine monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_01220};
DE            Short=UMP kinase {ECO:0000256|HAMAP-Rule:MF_01220};
DE            Short=UMPK {ECO:0000256|HAMAP-Rule:MF_01220};
GN   Name=pyrH {ECO:0000256|HAMAP-Rule:MF_01220,
GN   ECO:0000313|EMBL:BAI60447.1};
GN   OrderedLocusNames=MCP_0375 {ECO:0000313|EMBL:BAI60447.1};
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI60447.1, ECO:0000313|Proteomes:UP000001882};
RN   [1] {ECO:0000313|Proteomes:UP000001882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC   {ECO:0000313|Proteomes:UP000001882};
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(2011).
CC   -!- FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP.
CC       {ECO:0000256|HAMAP-Rule:MF_01220, ECO:0000256|SAAS:SAAS00055194}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + UMP = ADP + UDP; Xref=Rhea:RHEA:24400,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:456216; EC=2.7.4.22; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01220, ECO:0000256|SAAS:SAAS01121989};
CC   -!- ACTIVITY REGULATION: Inhibited by UTP. {ECO:0000256|HAMAP-
CC       Rule:MF_01220}.
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC       UDP from UMP (UMPK route): step 1/1. {ECO:0000256|HAMAP-Rule:MF_01220,
CC       ECO:0000256|SAAS:SAAS00055190}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01220,
CC       ECO:0000256|SAAS:SAAS00055196}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01220,
CC       ECO:0000256|SAAS:SAAS00366683}.
CC   -!- SIMILARITY: Belongs to the UMP kinase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01220, ECO:0000256|SAAS:SAAS00558071}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01220}.
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DR   EMBL; AP011532; BAI60447.1; -; Genomic_DNA.
DR   STRING; 304371.MCP_0375; -.
DR   EnsemblBacteria; BAI60447; BAI60447; MCP_0375.
DR   KEGG; mpd:MCP_0375; -.
DR   PATRIC; fig|304371.9.peg.384; -.
DR   eggNOG; arCOG00858; Archaea.
DR   eggNOG; COG0528; LUCA.
DR   HOGENOM; HOG000047188; -.
DR   KO; K09903; -.
DR   OMA; MGGTHPG; -.
DR   UniPathway; UPA00159; UER00275.
DR   Proteomes; UP000001882; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0033862; F:UMP kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04253; AAK_UMPK-PyrH-Pf; 1.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   HAMAP; MF_01220_A; PyrH_A; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR011817; Uridylate_kinase.
DR   InterPro; IPR011818; Uridylate_kinase_arch/spir.
DR   Pfam; PF00696; AA_kinase; 1.
DR   PIRSF; PIRSF005650; Uridylate_kin; 1.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   TIGRFAMs; TIGR02076; pyrH_arch; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1YVH5.
DR   SWISS-2DPAGE; D1YVH5.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01220,
KW   ECO:0000256|SAAS:SAAS00444198};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01220, ECO:0000256|SAAS:SAAS00444203};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01220, ECO:0000256|SAAS:SAAS00055189,
KW   ECO:0000313|EMBL:BAI60447.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01220,
KW   ECO:0000256|SAAS:SAAS00444199};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01220,
KW   ECO:0000256|SAAS:SAAS00444200};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001882};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01220,
KW   ECO:0000256|SAAS:SAAS00444196}.
FT   DOMAIN          1..202
FT                   /note="AA_kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00696"
FT   NP_BIND         9..10
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   NP_BIND         113..119
FT                   /note="UMP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         43
FT                   /note="UMP; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         44
FT                   /note="ATP; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         48
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         65
FT                   /note="UMP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         139
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         145
FT                   /note="ATP; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         148
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
SQ   SEQUENCE   223 AA;  24041 MW;  9B7DB14A539997CA CRC64;
     MRIVIKVGGS AIAPSLEAKR FSEYAQVIRS LAKDHTVLVV VGGGTPAREY INVTKELKAS
     NALRDLIGIG VSRLNARLLI SAMNDAAYPE PPHDYQEASL AMYSGKIIIM GGVQPGQTTD
     AVAAILAEYV HADLLIRTTS VDGVYTADPR VDKNAKKIDH MTPQELLELV AKMEMTAGAN
     NIFDMLGAQI IKRSHIPMMI ISGQDPHNII DAVNGKKIGT LIK
//

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