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 Q50754

Entry ID Method Resolution Chain Position Source
AF-Q50754-F1 Predicted AlphaFoldDB

No variants for Q50754

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q50754

No associated diseases with Q50754

No regional properties for Q50754

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q50754

Functions

Description
EC Number 1.8.98.5 With other, known, acceptors
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
4 iron, 4 sulfur cluster binding Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
CoB--CoM heterodisulfide reductase activity Catalysis of the reaction: coenzyme B + coenzyme M + methanophenazine = N-{7-[(2-sulfoethyl)dithio]heptanoyl}-3-O-phospho-L-threonine + dihydromethanophenazine.
metal ion binding Binding to a metal ion.

1 GO annotations of biological process

Name Definition
methanogenesis The chemical reactions and pathways resulting in the formation of methane, a colorless, odorless, flammable gas with the formula CH4. It is the simplest of the alkanes.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTLLQREENI IRKGNIDKEF SEKIKAAGGD SLEYCFQCGT CTGSCPSGRR TPYRVRQIIR
70 80 90 100 110 120
KANVGLKDEI ISDPTLWMCT TCYSCQERCP RKVKIVDVVK LARNEAAKAG FMAPAHKAVG
130 140 150 160 170 180
SFVIKTGHGV PINDATMELR KAVGLGELPP TTHQFPEALE EVQKIIKATG FDQLIGYNWE
TGELE