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 B2J6F7

Entry ID Method Resolution Chain Position Source
AF-B2J6F7-F1 Predicted AlphaFoldDB

No variants for B2J6F7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B2J6F7

No associated diseases with B2J6F7

2 regional properties for B2J6F7

Type Name Position InterPro Accession
domain Thiamine phosphate synthase/TenI 151 - 342 IPR022998
domain ThiD2 17 - 135 IPR041397

Functions

Description
EC Number 2.5.1.3 Transferring alkyl or aryl groups, other than methyl groups
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
magnesium ion binding Binding to a magnesium (Mg) ion.
thiamine-phosphate diphosphorylase activity Catalysis of the reaction: 4-amino-2-methyl-5-diphosphomethylpyrimidine + 4-methyl-5-(2-phosphoethyl)-thiazole + H(+) = diphosphate + thiamine phosphate.

2 GO annotations of biological process

Name Definition
thiamine biosynthetic process The chemical reactions and pathways resulting in the formation of thiamine (vitamin B1), a water soluble vitamin present in fresh vegetables and meats, especially liver.
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MVEPYSQKEQ VQQVVYRILD ANLDRAREGL RIIEEWCRFG LNNAQLALEC KRLRQELAKW
70 80 90 100 110 120
HTPELRAARD TPGDPGTELT HPQEEERASI KSVLQANFCR VEEALRVLEE YSKLYQPNIA
130 140 150 160 170 180
KACKQMRYQV YTLESNLMGH QRHQLLWRSR LYLVTSPSEN LLNNVEAALK GGLTLLQYRD
190 200 210 220 230 240
KTADDSLRLE QARKLRQLCH IYGALFIVND RVDLALAVDA DGVHLGQQDM PIAIARQLLG
250 260 270 280 290 300
SQRLIGLSTT NKEEMQAAIA EGVDYIGVGP VYETPTKVGK AATGLEYVSY AAKNCSIPWF
310 320 330 340 350
AIGGIDANNI NDAIDAGAKR VAVVRSLMQA EQPTLVTQYL LSQLNRIKPE L