A0A0U4B3X5 · A0A0U4B3X5_9CAUD

  • Protein
    N6-succino-2-amino-2'-deoxyadenylate synthase
  • Gene
    50
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Involved in the synthesis of the atypical nucleotide dZTP (2-amino-2'-deoxyadenosine-5'-triphosphate). Catalyzes the condensation of aspartate with deoxyguanylate into dSMP (N6-succino-2-amino-2'-deoxyadenylate), which undergoes defumarylation and phosphorylation respectively by host PurB and guanylate/nucleoside diphosphate kinases to give dZTP. dZTP is integrated into the viral genome instead of adenine by the viral DNA polymerase. This Z-base probably completely replaces adenosine and forms a triple bond to the opposite T-base. The resulting non-standard viral DNA is called Z-genome. The chemically modified DNA is probably harder for the host bacteria to digest with nucleases or restriction enzymes.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Pathway

Purine metabolism.

Features

Showing features for active site, binding site.

Type
IDPosition(s)Description
Active site14Proton acceptor
Binding site14ATP (UniProtKB | ChEBI)
Binding site14Mg2+ (UniProtKB | ChEBI)
Binding site14dGMP (UniProtKB | ChEBI)
Binding site17ATP (UniProtKB | ChEBI)
Binding site18ATP (UniProtKB | ChEBI)
Binding site44dGMP (UniProtKB | ChEBI)
Binding site46ATP (UniProtKB | ChEBI)
Binding site46Mg2+ (UniProtKB | ChEBI)
Binding site47ATP (UniProtKB | ChEBI)
Binding site48ATP (UniProtKB | ChEBI)
Binding site130dGMP (UniProtKB | ChEBI)
Binding site131dGMP (UniProtKB | ChEBI)
Binding site145dGMP (UniProtKB | ChEBI)
Binding site192ATP (UniProtKB | ChEBI)
Binding site207dGMP (UniProtKB | ChEBI)
Binding site269L-aspartate (UniProtKB | ChEBI)
Binding site269Mg2+ (UniProtKB | ChEBI)
Binding site270L-aspartate (UniProtKB | ChEBI)
Binding site275L-aspartate (UniProtKB | ChEBI)
Binding site359ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionadenylosuccinate synthase activity
Molecular FunctionATP binding
Molecular Functionmagnesium ion binding
Biological Process'de novo' AMP biosynthetic process
Biological ProcessIMP metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    N6-succino-2-amino-2'-deoxyadenylate synthase
  • EC number
  • Alternative names
    • 2-amino-2'-deoxyadenylo-succinate synthase
    • PurZ

Gene names

    • Name
      50
    • Synonyms
      purZ
    • ORF names
      JOANN_50

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Viruses > Duplodnaviria > Heunggongvirae > Uroviricota > Caudoviricetes > Korravirus > Korravirus joann

Accessions

  • Primary accession
    A0A0U4B3X5

Proteomes

Subcellular Location

Family & Domains

Sequence similarities

Belongs to the Caudovirales PurZ family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    377
  • Mass (Da)
    40,745
  • Last updated
    2016-03-16 v1
  • Checksum
    D9AE826275E9A8E3
MSNVMVVVGGQYGSEAKGHITAQLVKQAVQVGRHVVNVRVAGPNAGHTAYDDEGVKFAFRQVPVGAVIEPIVSVIAAGSEIDLPVLVEEIHLAQDNGHIIQLLIDENATLIEYHHKMQESEGKMVENIGSTAKGIGAARADRIWRRARRLRDSEAALELLRQISGVHVIDTVKYLHGQATQPNVNIIIEGTQGYGLGVHTDAYPQTTSSDCRAIDFLAMAGISPWHPGIEATQVIIACRVFPIRVAGNSGPMKGETSWEQLNLPEERTTVTQKVRRVGAWDGELVKAAFEANGGVAIDHDDMEGQLMQLVSGGPKVMVGLTMLDQVIPEIEGLTTFDDLDEPTLSKVEEWINKIYDETGAQVTMITTSPKTAVLLGA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KU160652
EMBL· GenBank· DDBJ
ALY09453.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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