A0A9P5SAJ3 · A0A9P5SAJ3_9FUNG

  • Protein
    Uridylate kinase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and dUMP as phosphate acceptors, but can also use CMP, dCMP and AMP.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per monomer.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site35-40ATP (UniProtKB | ChEBI)
Binding site61a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site83-85a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site145-148a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site152a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site183ATP (UniProtKB | ChEBI)
Binding site189a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site200a ribonucleoside 5'-phosphate (UniProtKB | ChEBI)
Binding site228ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
Molecular Function(d)CMP kinase activity
Molecular FunctionATP binding
Molecular FunctionUMP kinase activity
Biological Process'de novo' pyrimidine nucleobase biosynthetic process
Biological ProcessCDP biosynthetic process
Biological ProcessUDP biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Uridylate kinase
  • EC number
  • Short names
    UK
  • Alternative names
    • ATP:UMP phosphotransferase
    • Deoxycytidylate kinase
      (CK
      ; dCMP kinase
      )
    • Uridine monophosphate kinase
      (UMP kinase
      ; UMPK
      )

Gene names

    • ORF names
      BG006_001099

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • NVP1
  • Taxonomic lineage
    Eukaryota > Fungi > Fungi incertae sedis > Mucoromycota > Mortierellomycotina > Mortierellomycetes > Mortierellales > Mortierellaceae > Podila

Accessions

  • Primary accession
    A0A9P5SAJ3

Proteomes

Subcellular Location

Cytoplasm
Nucleus
Note: Predominantly cytoplasmic.

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region55-85NMPbind
Compositional bias106-121Basic and acidic residues
Region106-125Disordered
Region182-192LID

Domain

Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.

Sequence similarities

Belongs to the adenylate kinase family. UMP-CMP kinase subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    255
  • Mass (Da)
    28,996
  • Last updated
    2023-09-13 v1
  • Checksum
    E08786A44E540945
MFGSLYSKLLSAKKNYDKKRAFKQATVIFVLGGPGVGKGTQCARLVQEYGFIHLSAGDLLRQEQSRPGSPFYELISTFIAEGKIVPMEVTVALLENAILEHIQKANKEDKTKNEQETTKPEGTHSYIHSVFPRSHKKKVYFLVDGFPRQMDQAVRFEQEVTPCQFILYLEGPEDVMLERLLKRGETSGRADDNLESIKKRFTTFKETSYPVIEVYAKQGKVQTVSCVDGPDVVFENVKRVFNGQLFSGIEERREE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias106-121Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAAAUY010001200
EMBL· GenBank· DDBJ
KAF9323854.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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