ID A0A060SI48_PYCCI Unreviewed; 289 AA.
AC A0A060SI48;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Alpha-1,3/1,6-mannosyltransferase ALG2 {ECO:0000256|RuleBase:RU367136};
DE EC=2.4.1.132 {ECO:0000256|RuleBase:RU367136};
DE EC=2.4.1.257 {ECO:0000256|RuleBase:RU367136};
DE AltName: Full=GDP-Man:Man(1)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase {ECO:0000256|RuleBase:RU367136};
GN ORFNames=BN946_scf184940.g36 {ECO:0000313|EMBL:CDO71889.1};
OS Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=5643 {ECO:0000313|EMBL:CDO71889.1, ECO:0000313|Proteomes:UP000029665};
RN [1] {ECO:0000313|EMBL:CDO71889.1, ECO:0000313|Proteomes:UP000029665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM137 {ECO:0000313|EMBL:CDO71889.1,
RC ECO:0000313|Proteomes:UP000029665};
RA Levasseur A., Lomascolo A., Ruiz-Duenas F.J., Uzan E., Piumi F., Kues U.,
RA Ram A.F.J., Murat C., Haon M., Benoit I., Arfi Y., Chevret D., Drula E.,
RA Kwon M.J., Gouret P., Lesage-Meessen L., Lombard V., Mariette J.,
RA Noirot C., Park J., Patyshakuliyeva A., Wieneger R.A.B., Wosten H.A.B.,
RA Martin F., Coutinho P.M., de Vries R., Martinez A.T., Klopp C.,
RA Pontarotti P., Henrissat B., Record E.;
RT "The genome of the white-rot fungus Pycnoporus cinnabarinus: a
RT basidiomycete model with a versatile arsenal for lignocellulosic biomass
RT breakdown.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and
CC Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol
CC diphosphate. {ECO:0000256|RuleBase:RU367136}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC alpha-D-GlcNAc-diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-
CC (1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC alpha-D-GlcNAc-diphosphodolichol + GDP + H(+); Xref=Rhea:RHEA:29519,
CC Rhea:RHEA-COMP:12624, Rhea:RHEA-COMP:12626, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:132510,
CC ChEBI:CHEBI:132511; EC=2.4.1.257;
CC Evidence={ECO:0000256|RuleBase:RU367136};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-(1->3)-beta-D-
CC Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol +
CC GDP + H(+); Xref=Rhea:RHEA:29515, Rhea:RHEA-COMP:11044, Rhea:RHEA-
CC COMP:12624, ChEBI:CHEBI:15378, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:58472, ChEBI:CHEBI:132510; EC=2.4.1.132;
CC Evidence={ECO:0000256|RuleBase:RU367136};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|RuleBase:RU367136}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU367136}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC {ECO:0000256|RuleBase:RU367136}.
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:CDO71889.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CCBP010000108; CDO71889.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060SI48; -.
DR STRING; 5643.A0A060SI48; -.
DR HOGENOM; CLU_030619_2_0_1; -.
DR OMA; DENRCFE; -.
DR OrthoDB; 1377at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000029665; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004378; F:GDP-Man:Man1GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0102704; F:GDP-Man:Man2GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR InterPro; IPR027054; ALG2.
DR InterPro; IPR001296; Glyco_trans_1.
DR PANTHER; PTHR45918; ALPHA-1,3/1,6-MANNOSYLTRANSFERASE ALG2; 1.
DR PANTHER; PTHR45918:SF1; ALPHA-1,3_1,6-MANNOSYLTRANSFERASE ALG2; 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:RU367136};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU367136};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000029665};
KW Transferase {ECO:0000256|RuleBase:RU367136};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 147..261
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
SQ SEQUENCE 289 AA; 31536 MW; D341AC7E4BCCACB1 CRC64;
MDKLEEFTTT RVFKEQFPSI AVTPRVVYPG INLDAYGTGT VKLDDPDIAS VLSDRPTLLS
LNRFEQKKNA GLAIDSFALL RAKLASSPGD HPRKLRLVLA GGYDPRLLDN VKTLQSLLES
AKRHGLTYKV TTPSTSTVAS PALPFRKNSE KAPQETDILF LLNFSIGQRS ALLTSSSTLA
LLYTPANEHF GIGPVEGMAC GLPVLACDSG GPTESVVGAP VTERTGWLRR PEPKLWAEAL
LEIFNLSEEE RSQLAERARR RAREKFGMEA MARDLEDALQ KTAGMGPPS
//
