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 Q6NJL3

Entry ID Method Resolution Chain Position Source
AF-Q6NJL3-F1 Predicted AlphaFoldDB

No variants for Q6NJL3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6NJL3

No associated diseases with Q6NJL3

2 regional properties for Q6NJL3

Type Name Position InterPro Accession
domain Glycosyl transferase, family 1 214 - 385 IPR001296
domain Glycosyltransferase subfamily 4-like, N-terminal domain 24 - 203 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
MMTMRIAMIS IHTSPLQQPG SGDAGGMNVY IISIARELAR RGVDVDIYTR ATRPSQGDVV
70 80 90 100 110 120
EVESGLRVIN IVAGPYEGLS KEELPTQLAA FAGGVVQFAK CHHMRYDVIH SHYWLSGQVG
130 140 150 160 170 180
WLLRDLWNIP LVHTAHTLAA VKNAHRSAGD TEESEARRIC EQQLVDNADI LVVNTPEETN
190 200 210 220 230 240
DLVRHYDANP DSVAVIAPGA NVELFTPGTQ RNTEQSRRCL GIPLHTKVMA FVGRLQQFKG
250 260 270 280 290 300
PEVLLRAVAE MLERDPDRDM RVIMCGGPSG AAATVEHYIE LTRSLGIAHR VRFLDPRPPE
310 320 330 340 350 360
ELVSVYQAAD VVAVPSYNES FGLVAMEAQA SGTPVVAARV GGLPIAVVDG ETGVLVDGHD
370 380 390 400 410 420
PIMWADALEQ LLDDDPTRQQ MGVAAVEHAA NFTWAAAAEK LESVYGDAAM LDVAQCHDRY
AAGSDRA