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 A8GAB2

Entry ID Method Resolution Chain Position Source
AF-A8GAB2-F1 Predicted AlphaFoldDB

No variants for A8GAB2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A8GAB2

No associated diseases with A8GAB2

1 regional properties for A8GAB2

Type Name Position InterPro Accession
domain Aminoglycoside phosphotransferase 33 - 263 IPR002575

Functions

Description
EC Number 2.7.1.100 Phosphotransferases with an alcohol group 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
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
S-methyl-5-thioribose kinase activity Catalysis of the reaction: S-methyl-5-thio-D-ribose + ATP = S-methyl-5-thio-alpha-D-ribose 1-phosphate + ADP + 2 H(+).

3 GO annotations of biological process

Name Definition
L-methionine salvage from methylthioadenosine The generation of L-methionine (2-amino-4-(methylthio)butanoic acid) from methylthioadenosine.
L-methionine salvage from S-adenosylmethionine The chemical reactions and pathways resulting in the formation of L-methionine from S-adenosylmethionine.
phosphorylation The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSHYRTFTAA DAVEYARQYG QLADPQALVS ADEIGDGNLN LVFKIRDRDG VSRVIVKQAL
70 80 90 100 110 120
PYVRCVGESW PLTLDRARIE AETLLIHGGF CPRHTVKVLH HDAELAVMVQ EDLSDHHIWR
130 140 150 160 170 180
SELVKGHYYP LAAGQLAEYL AQTLFHTSDF YQTAQEKKAE VSRFSNPELC QITEDLFFTD
190 200 210 220 230 240
PYIDHERNQF DPALLPQVLE LRNDAALRLA VAGLKHRFLS KAEALLHGDI HSGSVFVAEG
250 260 270 280 290 300
KLKAIDAEFG FYGPIGFDVG TALGNLLLNY CGLPGLFGPR DAAAGREQRL QDVRELWLIF
310 320 330 340 350 360
ADRFLALCHQ QTREAALAVP GYAEQFLQQV WTDAVGYCGS ELIRRTIGLA HVADLDSISD
370 380 390
AEMRAECQRN ALGLGRALIV NAPQIEHIDA LLARIRQNG