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 Q2YQ03

Entry ID Method Resolution Chain Position Source
AF-Q2YQ03-F1 Predicted AlphaFoldDB

No variants for Q2YQ03

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2YQ03

No associated diseases with Q2YQ03

1 regional properties for Q2YQ03

Type Name Position InterPro Accession
domain Riboflavin kinase domain, bacterial/eukaryotic 18 - 172 IPR015865

Functions

Description
EC Number 3.5.4.16 In cyclic amidines
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

3 GO annotations of molecular function

Name Definition
GTP binding Binding to GTP, guanosine triphosphate.
GTP cyclohydrolase I activity Catalysis of the reaction: GTP + H2O = formate + 7,8-dihydroneopterin 3'-triphosphate.
zinc ion binding Binding to a zinc ion (Zn).

3 GO annotations of biological process

Name Definition
7,8-dihydroneopterin 3'-triphosphate biosynthetic process The chemical reactions and pathways resulting in the formation of 7,8-dihydroneopterin 3'-triphosphate.
one-carbon metabolic process The chemical reactions and pathways involving the transfer of one-carbon units in various oxidation states.
tetrahydrofolate biosynthetic process The chemical reactions and pathways resulting in the formation of tetrahydrofolate, 5,6,7,8-tetrahydrofolic acid, a folate derivative bearing additional hydrogens on the pterin group.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MDARILQDND DTSLPVNQAS VTRIHKKPGK AEAEAAVRTL LLWAGEDPDR EGLLETPKRV
70 80 90 100 110 120
AKAYQELFGG YSESPEEVLG TTFEEVAGYD DMVLVKDISF FSHCEHHMVP IIGKAHVAYL
130 140 150 160 170 180
PEGRVVGLSK IARVVDIFAR RLQTQESITA QIADSIQRIL KPRGVAVMIE AEHMCMAMRS
190 200 210
IRKQGSSTIT TTFTGDFKEK ADQQVRFMTL IRT