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 B1VEI4

Entry ID Method Resolution Chain Position Source
AF-B1VEI4-F1 Predicted AlphaFoldDB

No variants for B1VEI4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B1VEI4

No associated diseases with B1VEI4

2 regional properties for B1VEI4

Type Name Position InterPro Accession
domain Glycosyl transferase, family 1 211 - 385 IPR001296
domain Glycosyltransferase subfamily 4-like, N-terminal domain 22 - 196 IPR028098

Functions

Description
EC Number 2.4.1.250 Hexosyltransferases
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
acetylglucosaminyltransferase activity Catalysis of the transfer of an N-acetylglucosaminyl residue from UDP-N-acetyl-glucosamine to a sugar.
D-inositol-3-phosphate glycosyltransferase activity Catalysis of the reaction: UDP-N-acetyl-alpha-D-glucosamine + 1D-myo-inositol 3-phosphate = 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside 3-phosphate + UDP + H+.
magnesium ion binding Binding to a magnesium (Mg) ion.

1 GO annotations of biological process

Name Definition
mycothiol biosynthetic process The chemical reactions and pathways resulting in the formation of mycothiol, which consists of N-acetyl-L-cysteine linked to a pseudodisaccharide, D-glucosamine and myo-inositol. Mycothiol is produced in actinomycetes like mycobacteria and serves similar functions to glutathione.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MRIAMISMHT SPLEQAGTGD AGGMNVYIRN TAEQLAKLGL SVDIFTRATR PLQGEVVELG
70 80 90 100 110 120
DGVRVINCVA GPYEGLSKEE LPTQLAAFTG SVLAFTRQHG LSYDLIHSHY WLSGQVAWLL
130 140 150 160 170 180
RDLWNIRWVH TPHTLAAVKN NYLSEGDHRE PESRRICEQQ IVDNADVLIV NTDAEVADVE
190 200 210 220 230 240
EGYDSHKARI AVVTPGADIE KFTPGTERAT ENARRALGIP LSAKVIGFVG RLQRLKGPHV
250 260 270 280 290 300
LLQAAATLIE RYPDMPIRVL ICGGPSGSGL ERPKCLEELA EELGISRAVR FLKPRPPEEL
310 320 330 340 350 360
VSIYQAADVV AMPSANESFG LVALEAQATG TPVVATRIGG LQAAVAEGKS GLLVDGQDPQ
370 380 390 400 410 420
AWADALGQLL SDDDQRIAMA EYAPQHAARY SWENTAKQLV ELYRSLPTMP EEGPAERHPA
GSAN