ID F9XNK7_ZYMTI Unreviewed; 553 AA.
AC F9XNK7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
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 Name=ALG {ECO:0000313|EMBL:EGP82888.1};
GN ORFNames=MYCGRDRAFT_111451 {ECO:0000313|EMBL:EGP82888.1};
OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS fungus) (Septoria tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP82888.1, ECO:0000313|Proteomes:UP000008062};
RN [1] {ECO:0000313|EMBL:EGP82888.1, ECO:0000313|Proteomes:UP000008062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT reveals dispensome structure, chromosome plasticity, and stealth
RT pathogenesis.";
RL PLoS Genet. 7:E1002070-E1002070(2011).
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}.
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DR EMBL; CM001207; EGP82888.1; -; Genomic_DNA.
DR RefSeq; XP_003847912.1; XM_003847864.1.
DR AlphaFoldDB; F9XNK7; -.
DR STRING; 336722.F9XNK7; -.
DR EnsemblFungi; Mycgr3T111451; Mycgr3P111451; Mycgr3G111451.
DR GeneID; 13401675; -.
DR KEGG; ztr:MYCGRDRAFT_111451; -.
DR VEuPathDB; FungiDB:ZTRI_12.154; -.
DR eggNOG; KOG1387; Eukaryota.
DR HOGENOM; CLU_017896_1_1_1; -.
DR InParanoid; F9XNK7; -.
DR OMA; ARLYGWV; -.
DR OrthoDB; 197751at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008062; Chromosome 12.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004377; F:GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:EnsemblFungi.
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:UP000008062};
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 103..309
FT /note="ALG11 mannosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF15924"
FT DOMAIN 345..518
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT REGION 54..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 553 AA; 61447 MW; FB8041356092E768 CRC64;
MAVLITLLSV LLGLAVLTRL FPYAFRLLGR TIGNSIRSKT LHRREILLTR AVAEETDQKS
TTTKPTASSA SLDSDWEKVS SNGTQTPKSS PTTTSSDSSY SGVIAFFHPF CNAGGGGERV
LFAAILATQQ RYPNALCVVY TGDHDASRDQ ILANARNRFN IHLQPSRVVF LYLTTREWVL
ASKWPRFTLL GQSIGSLILG WDAFTLLAPD IMIDTMGYAF VLALSKWLFP SVPTAAYVHY
PTISTDMLQS LNSTDGSQGL NAGSGKGFRG LAKQFYWQKF ASLYSWVGGS VDIVMTNSSW
TQSHISTLWK PSRASQQPSP RPITVVYPPC AVAELQEKIP VTLENEKDRQ PHILYIAQFR
PEKMHTTIID AFHTFLREHH SSTPPSSRPR LILVGSVRDD HDEKRVYKLR LQAQEVKDSV
DFVVNAKWPQ ILEFLKSSKV GVNGMWNEHF GIGVVEYQAA GLVAVVNDSG GPKADIVVEV
DGGRTGFHAT TPKEFADGFA QALALKDEEA YAMRCRARKS SWRFSEEVFI EAWTKELVGL
VHLTNEDGQR KDI
//
