Q75BA5

PR
Gene name
ALG1 (ADL338C)
Protein name
Chitobiosyldiphosphodolichol beta-mannosyltransferase
Names
Asparagine-linked glycosylation protein 1, Beta-1,4-mannosyltransferase, GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase, GDP-mannose-dolichol diphosphochitobiose mannosyltransferase
Species
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
KEGG Pathway
ago:AGOS_ADL338C
EC number
2.4.1.142: Hexosyltransferases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-46 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q75BA5

Entry ID Method Resolution Chain Position Source
AF-Q75BA5-F1 Predicted AlphaFoldDB

No variants for Q75BA5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q75BA5

No associated diseases with Q75BA5

2 regional properties for Q75BA5

Type Name Position InterPro Accession
domain Glycosyl transferase, family 1 288 - 446 IPR001296
domain Glycosyltransferase subfamily 4-like, N-terminal domain 75 - 245 IPR028098

Functions

Description
EC Number 2.4.1.142 Hexosyltransferases
Subcellular Localization
  • Endoplasmic reticulum membrane ; Single-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.

2 GO annotations of molecular function

Name Definition
chitobiosyldiphosphodolichol beta-mannosyltransferase activity Catalysis of the reaction: GDP-mannose + chitobiosyldiphosphodolichol = GDP + beta-D-mannosylchitobiosyldiphosphodolichol.
mannosyltransferase activity Catalysis of the transfer of a mannosyl group to an acceptor molecule, typically another carbohydrate or a lipid.

3 GO annotations of biological process

Name Definition
oligosaccharide-lipid intermediate biosynthetic process The chemical reactions and pathways resulting in the formation of an oligosaccharide-lipid intermediate, such as a molecule of dolichol-P-man or dolicol-P-Glc used in N-linked glycosylation.
protein glycosylation A protein modification process that results in the addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid, e.g. the addition of glycan chains to proteins.
protein N-linked glycosylation A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the N4 atom of peptidyl-asparagine, the omega-N of arginine, or the N1' atom peptidyl-tryptophan.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MDTSSVTMHT ERACCHQAQR AVAAMLDKAP SWLIWTAVLY VGLPFMLYWA VPYLFYHNKT
70 80 90 100 110 120
KSRRIAIYVL GDLGHSPRIC YHARSFSAAG WEVELCGYLE EQPPKDLLDD PRVTIRALPG
130 140 150 160 170 180
ASNAGKSLGQ TARKVVLQTC HIVRQLWELR GCDYILIQNP PSIPLLPIVA IFKVLTRTRL
190 200 210 220 230 240
ILDWHNFAYT VLQLRVGRFL HPLVLVSYAV EFLFSRMADY HITVTAAMKD YLVQSFLLPA
250 260 270 280 290 300
RRIAVMYDRP GEQFRPLPAG ERGAALAEPF IRGYIPAGFD VQRGDTILVT STSFTLDEDI
310 320 330 340 350 360
NVLFGALKIY ESAAAKFDTT LPRILLFVTG KGPLKGKYME EVRNYKWERC TIHFLWLSAE
370 380 390 400 410 420
DYPRLLQLCD FGVSLHTSTS GLDLPMKVLD MFGSGLPAFV MDYPAIGELV QDRVNGLRFT
430 440 450 460 470
TRRELEQCLI FAIKDEHTRK VLKENALLES KNRWHQSWAS AMSELQVVRQ S