ID   B2AVY9_PODAN            Unreviewed;       501 AA.
AC   B2AVY9;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   02-SEP-2026, entry version 75.
DE   RecName: Full=Alpha-1,3-glucosyltransferase {ECO:0000256|RuleBase:RU363110};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU363110};
OS   Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS   (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC   Podospora anserina.
OX   NCBI_TaxID=515849 {ECO:0000313|EMBL:CDP32037.1, ECO:0000313|Proteomes:UP000001197};
RN   [1] {ECO:0000313|EMBL:CDP32037.1, ECO:0000313|Proteomes:UP000001197}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197};
RX   PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA   Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA   Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA   Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA   Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA   de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA   El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA   Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT   "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL   Genome Biol. 9:R77.1-R77.22(2008).
RN   [2] {ECO:0000313|Proteomes:UP000001197}
RP   GENOME REANNOTATION.
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197};
RX   PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA   Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA   Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Genetics 197:421-432(2014).
CC   -!- FUNCTION: Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-
CC       glucosyltransferase that operates in the biosynthetic pathway of
CC       dolichol-linked oligosaccharides, the glycan precursors employed in
CC       protein asparagine (N)-glycosylation. The assembly of dolichol-linked
CC       oligosaccharides begins on the cytosolic side of the endoplasmic
CC       reticulum membrane and finishes in its lumen. The sequential addition
CC       of sugars to dolichol pyrophosphate produces dolichol-linked
CC       oligosaccharides containing fourteen sugars, including two GlcNAcs,
CC       nine mannoses and three glucoses. Once assembled, the oligosaccharide
CC       is transferred from the lipid to nascent proteins by
CC       oligosaccharyltransferases. In the lumen of the endoplasmic reticulum,
CC       adds the second glucose residue from dolichyl phosphate glucose (Dol-P-
CC       Glc) onto the lipid-linked oligosaccharide intermediate
CC       Glc(1)Man(9)GlcNAc(2)-PP-Dol to produce Glc(2)Man(9)GlcNAc(2)-PP-Dol.
CC       {ECO:0000256|ARBA:ARBA00044725}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-
CC         alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-
CC         Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC         beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-
CC         dolichol + a di-trans,poly-cis-dolichyl beta-D-glucosyl phosphate =
CC         an alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-
CC         Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC         [alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-
CC         Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-
CC         trans,poly-cis-dolichol + a di-trans,poly-cis-dolichyl phosphate +
CC         H(+); Xref=Rhea:RHEA:31307, Rhea:RHEA-COMP:19498, Rhea:RHEA-
CC         COMP:19502, Rhea:RHEA-COMP:19521, Rhea:RHEA-COMP:19522,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683,
CC         ChEBI:CHEBI:132521, ChEBI:CHEBI:132522; EC=2.4.1.265;
CC         Evidence={ECO:0000256|ARBA:ARBA00047346};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31308;
CC         Evidence={ECO:0000256|ARBA:ARBA00047346};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU363110}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363110}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC       ECO:0000256|RuleBase:RU363110}.
CC   -!- SIMILARITY: Belongs to the ALG6/ALG8 glucosyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00008715, ECO:0000256|RuleBase:RU363110}.
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DR   EMBL; FO904942; CDP32037.1; -; Genomic_DNA.
DR   RefSeq; XP_001907890.1; XM_001907855.1.
DR   AlphaFoldDB; B2AVY9; -.
DR   STRING; 515849.B2AVY9; -.
DR   GeneID; 6192438; -.
DR   KEGG; pan:PODANSg4925; -.
DR   VEuPathDB; FungiDB:PODANS_7_5350; -.
DR   eggNOG; KOG2576; Eukaryota.
DR   HOGENOM; CLU_022045_1_1_1; -.
DR   OrthoDB; 1689333at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000001197; Chromosome 7.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042283; F:dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IEA:TreeGrafter.
DR   InterPro; IPR004856; Glyco_trans_ALG6/ALG8.
DR   PANTHER; PTHR12413; DOLICHYL GLYCOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR12413:SF2; DOLICHYL PYROPHOSPHATE GLC1MAN9GLCNAC2 ALPHA-1,3-GLUCOSYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF03155; Alg6_Alg8; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|RuleBase:RU363110};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU363110};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363110};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001197};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363110};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU363110};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU363110}.
FT   TRANSMEM        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363110"
FT   TRANSMEM        98..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363110"
FT   TRANSMEM        129..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363110"
FT   TRANSMEM        175..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363110"
FT   TRANSMEM        214..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363110"
FT   TRANSMEM        318..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363110"
FT   TRANSMEM        383..402
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363110"
FT   TRANSMEM        408..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363110"
FT   TRANSMEM        447..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363110"
FT   TRANSMEM        473..499
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363110"
SQ   SEQUENCE   501 AA;  56674 MW;  FE71141AB9DE8606 CRC64;
     MGEIYPTLAQ CAVVAAAFKI LLFPAYKSTD FEVHRNWLAI TNSLPLWEWY YEKTSEWTLD
     YPPFFAYFEW IMSQVAKLAD PAMLRVRNLE YASWETVYFQ RLTVIITELL LVYALQLFVD
     SSHGTSKRAA QAAAFSILLS PGLLIIDHIH FQYNGCMYGI LIWSLILARK KSTLLWSGLL
     FAALLCMKHI YLYLAPAYFV FLLRAYCLSP KSIFRIQFLN CVKLGGGIAA IFGVAFGPFA
     LKGQIPQILS RLFPFSRGLC HAYWAPNVWA IYSFVDRVLI VLAPRIGLSV KSSALQSVTR
     GLVGDTAFAV LPDITPQVCF ASTLIFQVIP LVRLFGQPTW DTFIGAVTLC GYASFLFGWH
     VHEKAILLVI IPFSLIALRD RRYLGAFRPL AVAGHVSLFP LLFTPAEFPI KTAYTIFWLI
     LFLMAFDRLA PASPRPRFFL FDRFSTLYIT VSIPLILYCS LLHGIIFGRS YEFLPLMFTS
     SYSAIGVVGS WVGFLVVYFT S
//