Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dolichyl N-acetyl-alpha-D-glucosaminyl phosphate 3-beta-D-2,3-diacetamido-2,3-dideoxy-beta-D-glucuronosyltransferase

Gene

aglC

Organism
Methanococcus voltae
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Involved in the assembly of an N-linked disaccharide that decorates the S-layer glycoprotein and flagellins (PubMed:18978056). AglC catalyzes the transfer of 2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronic acid (Glc-2,3-diNAcA) from uridine 5'-diphospho 2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronic acid (UDP-Glc-2,3-diNAcA) to the AglK product Dol-P-GlcNAc to yield Dol-P-GlcNAc-Glc-2,3-diNAcA (PubMed:23624439). AglC is specific for the monophosphate-linked Dol-P-GlcNAc (PubMed:23624439).2 Publications

Catalytic activityi

UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronate + an archaeal dolichyl N-acetyl-alpha-D-glucosaminyl phosphate = UDP + an archaeal dolichyl 3-O-(2,3-diacetamido-2,3-dideoxy-beta-D-glucuronsyl)-N-acetyl-alpha-D-glucosaminyl phosphate.1 Publication

Pathwayi: S-layer biogenesis

This protein is involved in the pathway S-layer biogenesis, which is part of Cell surface structure biogenesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway S-layer biogenesis and in Cell surface structure biogenesis.

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.1 Publication
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

  • transferase activity, transferring hexosyl groups Source: UniProtKB

GO - Biological processi

  • N-glycan processing Source: UniProtKB
  • protein glycosylation Source: UniProtKB-UniPathway
  • S-layer organization Source: UniProtKB-UniPathway

Keywordsi

Molecular functionGlycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-19264
UniPathwayiUPA00378
UPA00977

Protein family/group databases

CAZyiGT2 Glycosyltransferase Family 2

Names & Taxonomyi

Protein namesi
Recommended name:
Dolichyl N-acetyl-alpha-D-glucosaminyl phosphate 3-beta-D-2,3-diacetamido-2,3-dideoxy-beta-D-glucuronosyltransferase1 Publication (EC:2.4.1.3351 Publication)
Alternative name(s):
Glc-2,3-diNAcA glycosyltransferase1 Publication
UDP-Glc-2,3-diNAcA glycosyltransferase1 Publication
Gene namesi
Name:aglC1 Publication
OrganismiMethanococcus voltae
Taxonomic identifieri2188 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei252 – 272HelicalSequence analysisAdd BLAST21
Transmembranei290 – 310HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene result in flagellins and S-layer proteins with significantly reduced apparent molecular masses, loss of flagellar assembly and absence of glycan attachment.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004356541 – 321Dolichyl N-acetyl-alpha-D-glucosaminyl phosphate 3-beta-D-2,3-diacetamido-2,3-dideoxy-beta-D-glucuronosyltransferaseAdd BLAST321

Structurei

3D structure databases

ProteinModelPortaliB3VA59
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 2 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

KOiK21305

Family and domain databases

Gene3Di3.90.550.10, 1 hit
InterProiView protein in InterPro
IPR001173 Glyco_trans_2-like
IPR029044 Nucleotide-diphossugar_trans
PfamiView protein in Pfam
PF00535 Glycos_transf_2, 1 hit
SUPFAMiSSF53448 SSF53448, 1 hit

Sequencei

Sequence statusi: Complete.

B3VA59-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNFISIIIPT FNEEKYITKC LENWFNQDYP KENYEILIFD GKSTDKTLDV
60 70 80 90 100
IKELQKKHNF ENIKIYTNEK RKQVYAFNEG IKNANGDFFI IFGAHAYPEQ
110 120 130 140 150
DFLKNNIETY QRIKKEEPKL AGVGGIINKI SENMSAEIAK VIYSTPLSGG
160 170 180 190 200
SSFWYAKEGF FSNTVVYGMY DTKMIKESEI LFDTDFITGQ DFEFNLHLIK
210 220 230 240 250
EGFKLYTNPN IVSSYYTRSS VKKFIKQTIS YGAAKGLMIR KGYFNILWLF
260 270 280 290 300
PFGFLFMLLS IIITGLLIFI YIMAILIDTI RLLIKTREPL YIALPILLFL
310 320
FHCLISYGFF KGLIKGNSTF K
Length:321
Mass (Da):37,328
Last modified:September 2, 2008 - v1
Checksum:i4225C4DC1DB03D5A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU726231 Genomic DNA Translation: ACE74695.1

Genome annotation databases

KEGGiag:ACE74695

Similar proteinsi

Entry informationi

Entry nameiAGLC_METVO
AccessioniPrimary (citable) accession number: B3VA59
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 17, 2016
Last sequence update: September 2, 2008
Last modified: May 10, 2017
This is version 20 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health