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 Q83LH9

Entry ID Method Resolution Chain Position Source
AF-Q83LH9-F1 Predicted AlphaFoldDB

No variants for Q83LH9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q83LH9

No associated diseases with Q83LH9

1 regional properties for Q83LH9

Type Name Position InterPro Accession
domain Aminoglycoside phosphotransferase 25 - 221 IPR002575

Functions

Description
EC Number 2.7.1.89 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.
thiamine kinase activity Catalysis of the reaction: ATP + thiamine = ADP + 2 H(+) + thiamine phosphate.

3 GO annotations of biological process

Name Definition
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.
thiamine diphosphate biosynthetic process The chemical reactions and pathways resulting in the formation of thiamine diphosphate, a derivative of thiamine (vitamin B1) which acts as a coenzyme in a range of processes including the Krebs cycle.
thiamine metabolic process The chemical reactions and pathways involving thiamine (vitamin B1), a water soluble vitamin present in fresh vegetables and meats, especially liver.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MPFRSNNPIT RDELLSRFFP QFHPVTTFNS GLSGGSFLIE HQGQRFVVRQ PHDPDAPQSA
70 80 90 100 110 120
FLRQYRALSQ LPASIAPKPH LYLRDWMVVD YLPGAVKTYL PDTNELAGLL YYLHQQPRFG
130 140 150 160 170 180
WRITLLPLLE LYWQQSDPAR RTVGWLRMLK RLRKAREPRP LRLSPLHMDV HAGNLVHSAS
190 200 210 220 230 240
GLKLIDWEYA GDGDIALELA AVWVENTEQH RQLVNDYATR AKIYPAQLWR QVRRWFPWLL
250 260 270
MLKGGWFEYR WRQTGDQQFI RLADDTWRQL LIKQ