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Protein

Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase

Gene

alg3

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man5GlcNAc(2)-PP-Dol.By similarity

Catalytic activityi

Dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->3)-D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate.

Pathwayi: protein glycosylation

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
Recommended name:
Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase (EC:2.4.1.258)
Alternative name(s):
Asparagine-linked glycosylation protein 6
Dol-P-Man-dependent alpha(1-3)-mannosyltransferase
Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase
Gene namesi
Name:alg3
ORF Names:AO090120000319
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000006564 Componenti: Chromosome 5

Organism-specific databases

EuPathDBiFungiDB:AO090120000319.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1818LumenalSequence analysisAdd
BLAST
Transmembranei19 – 3921HelicalSequence analysisAdd
BLAST
Topological domaini40 – 9556CytoplasmicSequence analysisAdd
BLAST
Transmembranei96 – 11621HelicalSequence analysisAdd
BLAST
Topological domaini117 – 13923LumenalSequence analysisAdd
BLAST
Transmembranei140 – 16021HelicalSequence analysisAdd
BLAST
Topological domaini161 – 18121CytoplasmicSequence analysisAdd
BLAST
Transmembranei182 – 20221HelicalSequence analysisAdd
BLAST
Topological domaini203 – 2075LumenalSequence analysis
Transmembranei208 – 22821HelicalSequence analysisAdd
BLAST
Topological domaini229 – 26133CytoplasmicSequence analysisAdd
BLAST
Transmembranei262 – 28221HelicalSequence analysisAdd
BLAST
Topological domaini283 – 30422LumenalSequence analysisAdd
BLAST
Transmembranei305 – 32521HelicalSequence analysisAdd
BLAST
Topological domaini326 – 37247CytoplasmicSequence analysisAdd
BLAST
Transmembranei373 – 39321HelicalSequence analysisAdd
BLAST
Topological domaini394 – 41320LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 413413Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferasePRO_0000350923Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ2U6A4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ALG3 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000237555.
KOiK03845.
OMAiDWKAYMD.
OrthoDBiEOG76MKJK.

Family and domain databases

InterProiIPR007873. Glycosyltransferase_ALG3.
[Graphical view]
PANTHERiPTHR12646. PTHR12646. 1 hit.
PfamiPF05208. ALG3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2U6A4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELKHFIHEL CLNPRHTKWI APLLVIGDAF LCALIIWKIP YTEIDWTTYM
60 70 80 90 100
QQIALYISGE RDYTLIKGST GPLVYPAAHV YSYMALYHLT DEGRDILFGQ
110 120 130 140 150
ILFAVLYLVT LAVVMVCYRQ SGAPPYLFPL LVLSKRLHSV FVLRLFNDGL
160 170 180 190 200
AVCAMWIAIL LFQNKKWTAG VTAWTVGVGI KMTLLLLAPA IAVVTVLSLS
210 220 230 240 250
LVPSIRLGIL ALLIQVLLAI PFLQGNPIGY VARAFELTRQ FMFKWTVNWR
260 270 280 290 300
FVGEDLFLSK QFSLALLGLH IFLLGLFVTT GWLRPSGSNV PDFLRSLLQG
310 320 330 340 350
RQRTVVLSKS FIMTVMLTSL AIGLLCARSL HYQFFAYLSW ATPCLLWRAR
360 370 380 390 400
LHPILIYAIW ALQEWAWNVY PSTNASSSVV VFSLAVQVFG VLLNSRNALS
410
DAPPRRKGKE HIQ
Length:413
Mass (Da):46,649
Last modified:January 24, 2006 - v1
Checksum:iD73845A54C5E4F76
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007166 Genomic DNA. Translation: BAE62911.1.
RefSeqiXP_001824044.1. XM_001823992.2.

Genome annotation databases

EnsemblFungiiCADAORAT00011459; CADAORAP00011226; CADAORAG00011459.
GeneIDi5996303.
KEGGiaor:AOR_1_556094.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007166 Genomic DNA. Translation: BAE62911.1.
RefSeqiXP_001824044.1. XM_001823992.2.

3D structure databases

ProteinModelPortaliQ2U6A4.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAORAT00011459; CADAORAP00011226; CADAORAG00011459.
GeneIDi5996303.
KEGGiaor:AOR_1_556094.

Organism-specific databases

EuPathDBiFungiDB:AO090120000319.

Phylogenomic databases

HOGENOMiHOG000237555.
KOiK03845.
OMAiDWKAYMD.
OrthoDBiEOG76MKJK.

Enzyme and pathway databases

UniPathwayiUPA00378.

Family and domain databases

InterProiIPR007873. Glycosyltransferase_ALG3.
[Graphical view]
PANTHERiPTHR12646. PTHR12646. 1 hit.
PfamiPF05208. ALG3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequencing and analysis of Aspergillus oryzae."
    Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
    , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
    Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 42149 / RIB 40.

Entry informationi

Entry nameiALG3_ASPOR
AccessioniPrimary (citable) accession number: Q2U6A4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: January 24, 2006
Last modified: April 13, 2016
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.