A0A7S4AXR9 · A0A7S4AXR9_9STRA

Function

function

Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.
Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.

Caution

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

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Binds 1 divalent metal cation per subunit; can use either Mg2+ or Mn2+.
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.

Activity regulation

Activated by a monovalent cation that binds near, but not in, the active site. The most likely occupant of the site in vivo is potassium. Ion binding induces a conformational change that may alter substrate affinity.

Pathway

Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 2/2.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site82-84substrate
Binding site110-114substrate
Binding site217substrate
Binding site267ATP (UniProtKB | ChEBI)
Binding site306-311ATP (UniProtKB | ChEBI)
Binding site344K+ (UniProtKB | ChEBI)
Binding site346K+ (UniProtKB | ChEBI)
Binding site349-350ATP (UniProtKB | ChEBI)
Active site350Proton acceptor
Binding site350substrate
Binding site380K+ (UniProtKB | ChEBI)
Binding site383K+ (UniProtKB | ChEBI)
Binding site385K+ (UniProtKB | ChEBI)
Binding site389K+ (UniProtKB | ChEBI)
Binding site422-427ITP (UniProtKB | ChEBI)
Binding site455Mg2+ (UniProtKB | ChEBI)
Binding site467ITP (UniProtKB | ChEBI)
Binding site483Mg2+ (UniProtKB | ChEBI)
Binding site483-484ITP (UniProtKB | ChEBI)
Binding site559-562ITP (UniProtKB | ChEBI)
Binding site583ITP (UniProtKB | ChEBI)
Binding site588-589ITP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionnucleoside triphosphate diphosphatase activity
Molecular Functionribokinase activity
Biological ProcessD-ribose catabolic process
Biological Processdeoxyribonucleoside triphosphate catabolic process
Biological Processnucleotide metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Multifunctional fusion protein

Including 2 domains:

  • Recommended name
    Inosine triphosphate pyrophosphatase
  • EC number
  • Short names
    ITPase
    ; Inosine triphosphatase
  • Alternative names
    • Non-canonical purine NTP pyrophosphatase
    • Non-standard purine NTP pyrophosphatase
    • Nucleoside-triphosphate diphosphatase
    • Nucleoside-triphosphate pyrophosphatase
      (NTPase
      )
  • Recommended name
    Ribokinase
  • EC number
  • Short names
    RK

Gene names

    • ORF names
      PAUS00366_LOCUS22508

Organism names

  • Taxonomic identifier
  • Strain
    • 10249 10 AB
  • Taxonomic lineage
    Eukaryota > Sar > Stramenopiles > Ochrophyta > Bacillariophyta > Bacillariophyceae > Bacillariophycidae > Bacillariales > Bacillariaceae > Pseudo-nitzschia

Accessions

  • Primary accession
    A0A7S4AXR9

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain.

Type
IDPosition(s)Description
Signal1-24
ChainPRO_503139474525-607Multifunctional fusion protein

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain73-391Carbohydrate kinase PfkB

Sequence similarities

Belongs to the HAM1 NTPase family.
Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.
Belongs to the carbohydrate kinase pfkB family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    607
  • Mass (Da)
    65,651
  • Last updated
    2021-06-02 v1
  • MD5 Checksum
    4F64825368A546ADEFC89F7DAE82BB21
MRKCTHSVLPTLLLSLRASFPVKSFGPLPTFSTQPHKLKLSHRYSNHCHHSFRLTTARMSSTASENNNNDGNKLILVVGSANQDLTSTTAVFPTVGETVMGKNFATACGGKGANQAVAAASLNMAPVAMLCRVGDDLFGRNLMDNFRRVGVDCFDEKETIITDNEKCPSGVASILVNETSGDNMIVVSPGANYRLTQEDVRKTIAKAKPSQVLVQLEIRPPVVLEALKAGKDIGATTILNTAPAPEGWSLEDPEMNFFEHVDILILNETELRKVTGTSTSELPADDEESLAKSLITKGVGKAVIVTLGSRGAMIVEKIEDDGVTETVRVDAPEDLPGRKLPVKNTVGAGDSFCGALAAYRSAGLSLTEAAKYACGVASMTVRKDGAQTSYPLYDELPDCLKLKDRPSKRPKTSLKPIITFVTGNKKKLEEAKQILSTPDGSALFELSNKKIDLPELQGDAIEIAKEKCRLAAKEVNGAVFTEDTSLCFNALNGLPGPYIKWFLENCGHAGLNKMLDGFDDRSAYAQTILAYTTGPDEEIYIFDGRTTGKIVTARGPTDFGWDPVFEPDEGEGKTYAEMTKEFKNSISHRGRSFEKFRAFLAKSGSSD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HBIX01034442
EMBL· GenBank· DDBJ
CAE0729723.1
EMBL· GenBank· DDBJ
Transcribed RNA

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