ID A0A178EF07_9PLEO Unreviewed; 458 AA.
AC A0A178EF07;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=IQ07DRAFT_676328 {ECO:0000313|EMBL:OAL54245.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL54245.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL54245.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL54245.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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|ARBA:ARBA00003142,
CC 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|ARBA:ARBA00001514,
CC 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|ARBA:ARBA00001253,
CC ECO:0000256|RuleBase:RU367136};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922, 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 ---------------------------------------------------------------------------
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; KV441638; OAL54245.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178EF07; -.
DR STRING; 765867.A0A178EF07; -.
DR InParanoid; A0A178EF07; -.
DR OrthoDB; 1377at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000077535; 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 CDD; cd03805; GT4_ALG2-like; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR027054; ALG2.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR028098; Glyco_trans_4-like_N.
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; PF13439; Glyco_transf_4; 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 ECO:0000313|EMBL:OAL54245.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367136};
KW Reference proteome {ECO:0000313|Proteomes:UP000077535};
KW Transferase {ECO:0000256|RuleBase:RU367136, ECO:0000313|EMBL:OAL54245.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367136};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367136}.
FT TRANSMEM 433..457
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367136"
FT DOMAIN 19..204
FT /note="Glycosyltransferase subfamily 4-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13439"
FT DOMAIN 215..397
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
SQ SEQUENCE 458 AA; 50560 MW; FEC49C09FB67D0EF CRC64;
MAGDQPKQHI VFFHPDLGIG GAERLVIDAA VGLKNRGHKV TLFTSHRDLQ HCFDEARDGT
LDVRVRGNSL VPSTLLGRFA ILCAIARQLH LILQIALFSN ELQLLAPTTF FVDQLSAGVP
VLRLLLPRAR IIFYCHFPDK LLAKEGGILK SLYRRPFDWL ESWSTGCSDT IVVNSNFTKT
VFSQAFPSLS HRLPRVVYPC VDTSAATSNV GQKPLWDKKK VLLSINRFEK KKDIALALRA
YAGLSSIEQQ DARLVIAGGY DPRVPENVST YTELCDLADS LKLKHATAQS FTAAQGVPDD
IAVLFLHSID STFKATLLST SRLLIYTPLN EHFGIVPLEA MLAGTPVLAA NQGGPTETVI
SGQTGWLRDV SKTQDWTEVL RIALEDGDGE ERLKEMGKWG KQRVVADFSK EKLAERLELE
MNAMLSKDVR PQLVSMVFLL IPVGLLGTFV AVCLGLML
//
