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 Q2RGU4

Entry ID Method Resolution Chain Position Source
AF-Q2RGU4-F1 Predicted AlphaFoldDB

No variants for Q2RGU4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2RGU4

No associated diseases with Q2RGU4

No regional properties for Q2RGU4

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q2RGU4

Functions

Description
EC Number 3.5.1.2 In linear amides
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.

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
glutaminase activity Catalysis of the reaction: L-glutamine + H2O = L-glutamate + NH3.
phosphoribosylformylglycinamidine synthase activity Catalysis of the reaction: N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + ATP + H(2)O = 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate + ADP + 2 H(+) + phosphate.

2 GO annotations of biological process

Name Definition
'de novo' IMP biosynthetic process The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate, by the stepwise assembly of a purine ring on ribose 5-phosphate.
glutamine metabolic process The chemical reactions and pathways involving glutamine, 2-amino-4-carbamoylbutanoic acid.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKFGVIVFPG SNCDQDVHYA LGSVLGQNVD YLWHGDTSVS GYDCLILPGG FSYGDYLRAG
70 80 90 100 110 120
AIARFAPIMP AVIDFARSGG LVLGICNGFQ ILLEAGLLPG AMMRNACLQF RCQWTCLKVD
130 140 150 160 170 180
NNATPFTNRF REGQVVRIPI AHGEGNYYAD AATLAQLEAN RQIIFRYCSP DGEVTPAANP
190 200 210 220 230
NGSVGNIAGI INREGNVLGM MPHPERCAEG ILGGSDGREL LASIVDWWER GERLGA