ID Q6BUG4_DEBHA Unreviewed; 584 AA.
AC Q6BUG4;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Mannosyltransferase {ECO:0000256|RuleBase:RU363075};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU363075};
GN OrderedLocusNames=DEHA2C10868g {ECO:0000313|EMBL:CAG86226.1};
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG86226.1, ECO:0000313|Proteomes:UP000000599};
RN [1] {ECO:0000313|EMBL:CAG86226.1, ECO:0000313|Proteomes:UP000000599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC 2968 {ECO:0000313|Proteomes:UP000000599};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-
CC (1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a
CC dolichyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (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-diphosphodolichol + H(+);
CC Xref=Rhea:RHEA:29539, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:12630, Rhea:RHEA-COMP:12631, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:132519,
CC ChEBI:CHEBI:132520; EC=2.4.1.261;
CC Evidence={ECO:0000256|ARBA:ARBA00034020};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-alpha-D-
CC Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC diphosphodolichol = a dolichyl phosphate + alpha-D-Man-(1->2)-alpha-
CC D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-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 + H(+); Xref=Rhea:RHEA:29531,
CC Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527, Rhea:RHEA-COMP:12628,
CC Rhea:RHEA-COMP:12629, ChEBI:CHEBI:15378, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:58211, ChEBI:CHEBI:132516, ChEBI:CHEBI:132517;
CC EC=2.4.1.259; Evidence={ECO:0000256|ARBA:ARBA00033991};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363075}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU363075}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 22 family.
CC {ECO:0000256|ARBA:ARBA00007063, ECO:0000256|RuleBase:RU363075}.
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DR EMBL; CR382135; CAG86226.1; -; Genomic_DNA.
DR RefSeq; XP_458155.1; XM_458155.1.
DR AlphaFoldDB; Q6BUG4; -.
DR STRING; 284592.Q6BUG4; -.
DR CAZy; GT22; Glycosyltransferase Family 22.
DR GeneID; 2900304; -.
DR KEGG; dha:DEHA2C10868g; -.
DR VEuPathDB; FungiDB:DEHA2C10868g; -.
DR eggNOG; KOG2515; Eukaryota.
DR HOGENOM; CLU_018152_0_0_1; -.
DR InParanoid; Q6BUG4; -.
DR OMA; PRDMHAK; -.
DR OrthoDB; 162888at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000599; Chromosome C.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0052926; F:dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0052918; F:dol-P-Man:Man(8)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR005599; GPI_mannosylTrfase.
DR PANTHER; PTHR22760:SF2; ALPHA-1,2-MANNOSYLTRANSFERASE ALG9; 1.
DR PANTHER; PTHR22760; GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF03901; Glyco_transf_22; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU363075};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU363075};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363075};
KW Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363075};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363075}.
FT TRANSMEM 20..37
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 185..213
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 225..248
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 281..307
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 314..333
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 345..372
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 384..402
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
SQ SEQUENCE 584 AA; 65883 MW; FE61CD539308479C CRC64;
MSSKTNVGES QRLNGLQIGL IALNVLLRVY AAFFMIISDC DETFNYWEPL NLLIRGFGKQ
TWEYSPDYAI RSYTYLIPYV IVTYPIKVFE KFVNIPSYYQ FYWIRLIALC GFTCFTELRL
FYSINSSLNR KVGNWFLFLS SIAPGMSHAG VALLPSSFAM NCVTMATANS LSAISENSAN
YSVQAIIWFL VGGIVGWPFA LALGLPFGLF ILIQNIKRFN VLFSIIKGCI AGLVSTLIIS
TAIDSWFYQK LDLVPLNIVL YNVFGEQGEG PEIFGVEPFH YYILNLLVNF NVVAILGYVG
LVMNVVLFGE KNRYKVLITV SLPLLIWSLI FGSQPHKEER FLYPVYPLLI LSSSLLLTLI
FPMVTFVSKG IAANKINSKH IEKLVQLLFA FSVGMVSILR IINLVENYST PLSVHREIST
LPVSNISVNV CTGREWYHFP NSFFLPDNYR LKFIRSGFDG LLPGDFLEGA SLKASTSSIP
PNMNNKNQYS DDKVIDFDEC SYYIDNSQAA NLEVGEPNIV ERSGKELKVN KGWSVVQCQN
IINPSGTSSG IGKLLWIPEY VRSLIPYNVD YMDYCLVERK KNIV
//
