ID Q4WJ82_ASPFU Unreviewed; 560 AA.
AC Q4WJ82;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 24-JAN-2024, entry version 87.
DE RecName: Full=GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase {ECO:0000256|ARBA:ARBA00022018, ECO:0000256|RuleBase:RU367051};
DE EC=2.4.1.131 {ECO:0000256|ARBA:ARBA00012645, ECO:0000256|RuleBase:RU367051};
GN ORFNames=AFUA_1G06890 {ECO:0000313|EMBL:EAL88400.1};
OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS Af293) (Neosartorya fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL88400.1, ECO:0000313|Proteomes:UP000002530};
RN [1] {ECO:0000313|EMBL:EAL88400.1, ECO:0000313|Proteomes:UP000002530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC {ECO:0000313|Proteomes:UP000002530};
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- FUNCTION: Required for N-linked oligosaccharide assembly. Has a role in
CC the last step of the synthesis of the Man(5)GlcNAc(2)-PP-dolichol core
CC oligosaccharide on the cytoplasmic face of the endoplasmic reticulum.
CC {ECO:0000256|ARBA:ARBA00024788}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + 2 GDP-alpha-
CC D-mannose = alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC [alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-
CC GlcNAc-diphosphodolichol + 2 GDP + 2 H(+); Xref=Rhea:RHEA:29523,
CC Rhea:RHEA-COMP:12626, Rhea:RHEA-COMP:12627, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:132511,
CC ChEBI:CHEBI:132515; EC=2.4.1.131;
CC Evidence={ECO:0000256|ARBA:ARBA00000841,
CC ECO:0000256|RuleBase:RU367051};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|RuleBase:RU367051}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU367051}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000256|RuleBase:RU367051}.
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:EAL88400.1}.
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DR EMBL; AAHF01000007; EAL88400.1; -; Genomic_DNA.
DR RefSeq; XP_750438.1; XM_745345.1.
DR AlphaFoldDB; Q4WJ82; -.
DR STRING; 330879.Q4WJ82; -.
DR EnsemblFungi; EAL88400; EAL88400; AFUA_1G06890.
DR GeneID; 3507697; -.
DR KEGG; afm:AFUA_1G06890; -.
DR VEuPathDB; FungiDB:Afu1g06890; -.
DR eggNOG; KOG1387; Eukaryota.
DR HOGENOM; CLU_017896_1_1_1; -.
DR InParanoid; Q4WJ82; -.
DR OMA; ARLYGWV; -.
DR OrthoDB; 197751at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002530; Chromosome 1.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0004377; F:GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR CDD; cd03806; GT4_ALG11-like; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR InterPro; IPR038013; ALG11.
DR InterPro; IPR031814; ALG11_N.
DR InterPro; IPR001296; Glyco_trans_1.
DR PANTHER; PTHR45919; GDP-MAN:MAN(3)GLCNAC(2)-PP-DOL ALPHA-1,2-MANNOSYLTRANSFERASE; 1.
DR PANTHER; PTHR45919:SF1; GDP-MAN:MAN(3)GLCNAC(2)-PP-DOL ALPHA-1,2-MANNOSYLTRANSFERASE; 1.
DR Pfam; PF15924; ALG11_N; 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:RU367051};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU367051}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367051};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 113..320
FT /note="ALG11 mannosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF15924"
FT DOMAIN 355..533
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT REGION 64..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 560 AA; 62504 MW; 315FA7320FE28775 CRC64;
MMLFLLKTFL TLLALLATCV LLPQFPLGVL RFVLRGVGWV IQKRTRSRRE FLISRVRADE
EEQLVKRSKS SPRGEDEDWE KVDSSSSSSG TAGPSKKGGN NGNKGPADAD WEGIIGFFHP
FCNAGGGGER VLWEAVRATQ RRWPKAICAI YTGDHEVNKM AMLERVENRF NIQLHAPAVV
LLYLTTRKYV LSSMYPYMTL LGQSLGSLVV AYDAFNLLVP DVFIDTMGYA FTLAFCKMLF
PSVPTGAYVH YPTISTDMLQ SLDDSTGLKG VNAGAGKGFK GQVKRKYWLA FARLYGWVGG
HVDVVMCNSS WTSAHIRTIW GPSRTSRTFK EPTVIFPPTA VSEIESTITV DEDSERSREP
IILYIAQFRP EKNHPLVLRS FARFLSERKT NPTSAALPQP KLVLMGSVRH SSPDETHIYN
LRLLAHELRI RDHTTFVCDA SWPTILSHLR SASVGVNAMW NEHFGICVVE YQAAGLISVV
HDSGGPREDI VIDLGDGATG FRASSEDEFA AAFEAALALP AEEKVAMRQR ARKSALRFTE
EEFSQKWIEE VGKLVEICRR
//
