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 A2BXM8

Entry ID Method Resolution Chain Position Source
AF-A2BXM8-F1 Predicted AlphaFoldDB

No variants for A2BXM8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A2BXM8

No associated diseases with A2BXM8

3 regional properties for A2BXM8

Type Name Position InterPro Accession
domain Oxoglutarate/iron-dependent dioxygenase 80 - 174 IPR005123
domain Prolyl 4-hydroxylase, alpha subunit 1 - 173 IPR006620
domain Prolyl 4-hydroxylase alpha subunit, Fe(2+) 2OG dioxygenase domain 91 - 172 IPR044862

Functions

Description
EC Number
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
2-oxoglutarate-dependent dioxygenase activity Catalysis of the reaction: A + 2-oxoglutarate + O2 = B + succinate + CO2. This is an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from 2-oxoglutarate and one other donor, and one atom of oxygen is incorporated into each donor.
iron ion binding Binding to an iron (Fe) ion.
L-ascorbic acid binding Binding to L-ascorbic acid, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate; L-ascorbic acid is vitamin C and has co-factor and anti-oxidant activities in many species.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MNFLTYKLLN LEELKILKLN LNKQNELWES GKMTAGSQAS KVKENLQLNR NSEISKKYSQ
70 80 90 100 110 120
LIRKKIITNP LIKSFALPKT IHGIMFTKSL QNMHYGRHID NPFMSSGRSD LSFTISLTNK
130 140 150 160 170 180
ADYQGGELVI ETLNSEKKLK LDAGEIIIYP STYLHSVKKV KNGERLVCVG WIESYVKSIE
190 200 210 220
EREYLFDLDA GAKGLLAKYG RSDELDNIFK SYSNLLRLLG N