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 Q9WWW2

Entry ID Method Resolution Chain Position Source
AF-Q9WWW2-F1 Predicted AlphaFoldDB

No variants for Q9WWW2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9WWW2

No associated diseases with Q9WWW2

2 regional properties for Q9WWW2

Type Name Position InterPro Accession
domain Glucose-methanol-choline oxidoreductase, N-terminal 2 - 295 IPR000172
domain Glucose-methanol-choline oxidoreductase, C-terminal 387 - 523 IPR007867

Functions

Description
EC Number
Subcellular Localization
  • Cell inner membrane
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

2 GO annotations of molecular function

Name Definition
alkan-1-ol dehydrogenase (acceptor) activity Catalysis of the reaction: primary alcohol + acceptor = aldehyde + reduced acceptor.
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.

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
MYDYIIVGAG SAGCVLANRL SADPSKRVCL LEAGPRDTNP LIHMPLGIAL LSNSKKLNWA
70 80 90 100 110 120
FQTAPQQHLN ERSLFWPRGK TLGGSSSINA MVYIRGHEED YQAWEQAGGE YWGWKRAFAL
130 140 150 160 170 180
FKKLEHNQRF DKSNYHGTDG ELAVSDLKDL NPLSKSFVQA GMEAKISFNG DFNGAHQEGV
190 200 210 220 230 240
GFYQVTQKHG QRWSSARAFL HDVIDRPNLD IITEAHATKV LFEDRKAVGV SYIQKNMHQQ
250 260 270 280 290 300
VKTTDSGEVI LSLGAVNTPQ LLMLSGVGAA AELKEHGIAL VHDLPEVGKN LQDHLDITLM
310 320 330 340 350 360
CAANSRTPIG VAFSFIPRGL VGLFSYIFKR KGFLTSNVAE SGGFVKSSPE RDRPNLQFHF
370 380 390 400 410 420
LPTYLKDHGR KIAVGYGYTL HICDLLPKSR GRIGLKSANP MDDPLIDPNY LSDPEDIKTM
430 440 450 460 470 480
IAGIKIGRAI FDAPSMAKHF KREIVPGPAV TSDDEIVADI RSRAETIYHP VGTCRMGKDP
490 500 510 520 530 540
ASVVDPCLQV RGLRNIRVVD ASIMPNLVAG NTNAPTIMIA ENAAEIIVRK VDMASLDASI
550
GFTRQNLEPE LL