ID A0A0L1KU89_9EUGL Unreviewed; 464 AA.
AC A0A0L1KU89;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=XU18_2003 {ECO:0000313|EMBL:KNH07471.1};
OS Perkinsela sp. CCAP 1560/4.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Prokinetoplastina;
OC Ichthyobodonidae; Perkinsela.
OX NCBI_TaxID=1314962 {ECO:0000313|EMBL:KNH07471.1, ECO:0000313|Proteomes:UP000036983};
RN [1] {ECO:0000313|EMBL:KNH07471.1, ECO:0000313|Proteomes:UP000036983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1560/4 {ECO:0000313|EMBL:KNH07471.1};
RA Tanifuji G., David V., Flegontov P., Gerasimov E., Hashimi H.,
RA Logacheva M., Maruyama S., Onodera N., Gray M., Archibald J., Curtis B.,
RA Cenci U., Lukes J.;
RT "Draft genomes of Paramoeba pemaquidensis and its kinetoplastid
RT endosymbiont Perkinsela sp. CCAP 1560/4.";
RL Submitted (JUN-2015) 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: Membrane {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:KNH07471.1}.
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DR EMBL; LFNC01000115; KNH07471.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L1KU89; -.
DR EnsemblProtists; KNH07471; KNH07471; XU18_2003.
DR OrthoDB; 1377at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000036983; Unassembled WGS sequence.
DR GO; GO:0016020; C: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 Glycosyltransferase {ECO:0000256|RuleBase:RU367136};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367136};
KW Reference proteome {ECO:0000313|Proteomes:UP000036983};
KW Transferase {ECO:0000256|RuleBase:RU367136, ECO:0000313|EMBL:KNH07471.1};
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 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367136"
FT TRANSMEM 119..138
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367136"
FT DOMAIN 261..443
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
SQ SEQUENCE 464 AA; 52041 MW; 18E80CECE036C990 CRC64;
MGVGASMGYF LLAIGIVIVL ARQIAQHRRT NLNSSQRSVI FIHPDLGIGG AERLVIDLAS
GLSHFHRCQT CILTTSFDES RCFAEVANSQ RSSKGNPSNS HLNVIVRGNS FPRSIQGRLV
RLCKSLSMVY AVTWLVLYGP VYEAFVVDQI SIALPILRLL LGNTPKIVFY CHFPDHLCNP
WKDHPSRVSR LVWTRVYTAL FNALEKWSFR FADIILFNSQ YTKAVAGKFL SVTGKVLYPP
MKGTAHESTK EVSKVPDMIK NLLSPKVFLI LSVSRFEPKK NPMLAVRMLA HIVQMARDAR
RIGFSQKNTP IHLVLCGGYD TRLMDNRVCM EEIQEWLTAH PTIKRKISIF TNISECIKWQ
LLHRADLVVY TPENEHFGIV PVEAMSCGKS VVASNTGGLL ETVGLSGVYG VLVDANPKCF
ATAVLELFND NSRRDQIGCD ARERVRSMFS LEKSSRSLYD ILFS
//
