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 Q5DYB5

Entry ID Method Resolution Chain Position Source
AF-Q5DYB5-F1 Predicted AlphaFoldDB

No variants for Q5DYB5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5DYB5

No associated diseases with Q5DYB5

3 regional properties for Q5DYB5

Type Name Position InterPro Accession
domain Pyridoxamine 5'-phosphate oxidase, putative 40 - 122 IPR011576
domain Pyridoxine 5'-phosphate oxidase, dimerisation, C-terminal 177 - 217 IPR019576
conserved_site Pyridoxamine 5'-phosphate oxidase, conserved site 187 - 200 IPR019740

Functions

Description
EC Number 1.4.3.5 With oxygen as acceptor
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

2 GO annotations of molecular function

Name Definition
FMN binding Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
pyridoxamine-phosphate oxidase activity Catalysis of the reaction: pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + hydrogen peroxide.

1 GO annotations of biological process

Name Definition
pyridoxine biosynthetic process The chemical reactions and pathways resulting in the formation of pyridoxine, 2-methyl-3-hydroxy-4,5-bis(hydroxymethyl)pyridine, one of the vitamin B6 compounds.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MELEDIRRDY SLGGLRRADL PQEPVELFEL WLKQAVEAKL TDPTAMTVAT VDENGQPFQR
70 80 90 100 110 120
IVLLKHFDKT GFVFYTNLGS RKAQQLEQHS KISLHFPWHP LERQVHITGT AEKLTALENM
130 140 150 160 170 180
KYFTSRPKES QIAAWASKQS SRLTARAALE GKYLELKQKF AKGEIPVPKF WGGFRIKIDS
190 200 210
IEFWQGGDHR LHDRFLYSKD QNDWQIDRLA P