ID A0A093X7T8_9PEZI Unreviewed; 561 AA.
AC A0A093X7T8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase {ECO:0000256|ARBA:ARBA00022018, ECO:0000256|RuleBase:RU367051};
DE EC=2.4.1.131 {ECO:0000256|ARBA:ARBA00012645, ECO:0000256|RuleBase:RU367051};
GN ORFNames=O988_08934 {ECO:0000313|EMBL:KFX88703.1};
OS Pseudogymnoascus sp. VKM F-3808.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1391699 {ECO:0000313|EMBL:KFX88703.1, ECO:0000313|Proteomes:UP000029329};
RN [1] {ECO:0000313|EMBL:KFX88703.1, ECO:0000313|Proteomes:UP000029329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3808 {ECO:0000313|EMBL:KFX88703.1,
RC ECO:0000313|Proteomes:UP000029329};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for N-linked oligosaccharide assembly. Has a role in
CC the last step of the synthesis of the Man(5)GlcNAc(2)-PP-dolichol core
CC oligosaccharide on the cytoplasmic face of the endoplasmic reticulum.
CC {ECO:0000256|ARBA:ARBA00024788}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + 2 GDP-alpha-
CC D-mannose = alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC [alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-
CC GlcNAc-diphosphodolichol + 2 GDP + 2 H(+); Xref=Rhea:RHEA:29523,
CC Rhea:RHEA-COMP:12626, Rhea:RHEA-COMP:12627, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:132511,
CC ChEBI:CHEBI:132515; EC=2.4.1.131;
CC Evidence={ECO:0000256|ARBA:ARBA00000841,
CC ECO:0000256|RuleBase:RU367051};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|RuleBase:RU367051}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU367051}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000256|RuleBase:RU367051}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFX88703.1}.
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DR EMBL; JPJR01002403; KFX88703.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093X7T8; -.
DR STRING; 1391699.A0A093X7T8; -.
DR HOGENOM; CLU_017896_1_1_1; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000029329; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004377; F:GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR CDD; cd03806; GT4_ALG11-like; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR InterPro; IPR038013; ALG11.
DR InterPro; IPR031814; ALG11_N.
DR InterPro; IPR001296; Glyco_trans_1.
DR PANTHER; PTHR45919; GDP-MAN:MAN(3)GLCNAC(2)-PP-DOL ALPHA-1,2-MANNOSYLTRANSFERASE; 1.
DR PANTHER; PTHR45919:SF1; GDP-MAN:MAN(3)GLCNAC(2)-PP-DOL ALPHA-1,2-MANNOSYLTRANSFERASE; 1.
DR Pfam; PF15924; ALG11_N; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU367051};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU367051};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367051};
KW Reference proteome {ECO:0000313|Proteomes:UP000029329};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367051};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367051};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367051}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367051"
FT DOMAIN 102..310
FT /note="ALG11 mannosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF15924"
FT DOMAIN 344..507
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
SQ SEQUENCE 561 AA; 62055 MW; 9082D5E38D0052C5 CRC64;
MIPLGLILGI TAVVMFLPIG LVLYGHALAQ ILGESIGWYL LKRSAPKRAI ILKKVAEEEA
ELAKETARGN KAKEGDEEWE KVESYAAGNA ENGDVAEKDW EGIVGFLHPF CNAGGGGERV
LWAAVRATQQ RWPKATCVVY TGDHDVTKEK MLERVENRFN IQLHAPTVTF LYLTTRHLVL
ASTWSFATLI GQSLGSLFMA YDAFSLVVPD IFVDTMGYAF ALGLCKLMFP KVPTGAYVHY
PTISTDMLAS LDSTSPSAHG VNAGKGAGTR GAAKKIYWEV FAKFYGWVGS SIDVVMTNST
WTQGHIRSLW GGFRADRGVM SEIAVVYPPV AVEELESEIE ISAASEKKRS KTLLYIAQFR
PEKNHTLILN SFAEFMRTKS PATKGAKLVL VGSVRDDADS KRVYELRLLA NELQIKNNVE
FHLDASWPEI LEWLRKASIG VNGMWNEHFG IGVVEYQAAG LVAVVHKSGG PKIDIVTEVD
GKPTGFHATT ATEFAEGFEK ALSLKDTLDW RRRARLSSKR FTEEEFAKRF IKQMETLVLL
QVNGPGPGKK IDTHLHEGFH M
//
