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

4 structures for Q6QWR1

Entry ID Method Resolution Chain Position Source
4MIF X-ray 180 A A/B/C/D 1-620 PDB
4MIG X-ray 180 A A/B/C/D 1-621 PDB
4MIH X-ray 240 A A/B/C/D/E/F/G/H 1-620 PDB
AF-Q6QWR1-F1 Predicted AlphaFoldDB

No variants for Q6QWR1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6QWR1

No associated diseases with Q6QWR1

1 regional properties for Q6QWR1

Type Name Position InterPro Accession
domain Glucose-methanol-choline oxidoreductase, C-terminal 486 - 608 IPR007867

Functions

Description
EC Number 1.1.3.10 With oxygen as acceptor
Subcellular Localization
  • Periplasm
  • Hyphal periplasmic space
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
periplasmic space The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria).

2 GO annotations of molecular function

Name Definition
flavin adenine dinucleotide binding Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
pyranose oxidase activity Catalysis of the reaction: D-glucose + O(2) = 2-dehydro-D-glucose + H(2)O(2).

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
MFLDTTPFRA DEPYDVFIAG SGPIGATFAK LCVDANLRVC MVEIGAADSF TSKPMKGDPN
70 80 90 100 110 120
APRSVQFGPG QVPIPGYHKK NEIEYQKDID RFVNVIKGAL STCSIPTSNN HIATLDPSVV
130 140 150 160 170 180
SNSLDKPFIS LGKNPAQNPF VNLGAEAVTR GVGGMSTHWT CATPEFFAPA DFNAPHRERP
190 200 210 220 230 240
KLSTDAAEDA RIWKDLYAQA KEIIGTSTTE FDHSIRHNLV LRKYNDIFQK ENVIREFSPL
250 260 270 280 290 300
PLACHRLTDP DYVEWHATDR ILEELFTDPV KRGRFTLLTN HRCTKLVFKH YRPGEENEVD
310 320 330 340 350 360
YALVEDLLPH MQNPGNPASV KKIYARSYVV ACGAVATAQV LANSHIPPDD VVIPFPGGEK
370 380 390 400 410 420
GSGGGERDAT IPTPLMPMLG KYITEQPMTF CQVVLDSSLM EVVRNPPWPG LDWWKEKVAR
430 440 450 460 470 480
HVEAFPNDPI PIPFRDPEPQ VTIKFTEEHP WHVQIHRDAF SYGAVAENMD TRVIVDYRFF
490 500 510 520 530 540
GYTEPQEANE LVFQQHYRDA YDMPQPTFKF TMSQDDRARA RRMMDDMCNI ALKIGGYLPG
550 560 570 580 590 600
SEPQFMTPGL ALHLAGTTRC GLDTQKTVGN THCKVHNFNN LYVGGNGVIE TGFAANPTLT
610 620
SICYAIRASN DIIAKFGRHR G