Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q03UJ4

Entry ID Method Resolution Chain Position Source
AF-Q03UJ4-F1 Predicted AlphaFoldDB

No variants for Q03UJ4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q03UJ4

No associated diseases with Q03UJ4

1 regional properties for Q03UJ4

Type Name Position InterPro Accession
domain Phosphoribosyltransferase domain 33 - 157 IPR000836

Functions

Description
EC Number 2.4.2.22 Pentosyltransferases
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

1 GO annotations of molecular function

Name Definition
xanthine phosphoribosyltransferase activity Catalysis of the reaction: 5-phospho-alpha-D-ribose 1-diphosphate + xanthine = (9-D-ribosylxanthine)-5'-phosphate + diphosphate.

3 GO annotations of biological process

Name Definition
purine ribonucleoside salvage Any process which produces a purine nucleoside from derivatives of it, without de novo synthesis.
xanthine metabolic process The chemical reactions and pathways involving xanthine, 2,6-dihydroxypurine, a purine formed in the metabolic breakdown of guanine but not present in nucleic acids.
XMP salvage Any process which produces xanthosine monophosphate from derivatives of it, without de novo synthesis.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKILEQRIKK DGRVLGKDVL KVDSFLNHQV DPELMQAMGE EFATIFSDEK IDKIVTVESS
70 80 90 100 110 120
GIAPAVFAGL ALHVPVVFAR KNKSLTLPEN VWTADVYSFT KQTTNHIMID HRFLSAAENI
130 140 150 160 170 180
LIIDDFLANG QAVEGLLKIA NDANANVVGV GVVIEKTFQK GRQILDERGV RVESLARIKG
FENDEVIFL