ID A0A0D1CG77_USTMA Unreviewed; 784 AA.
AC A0A0D1CG77;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Mannosyltransferase {ECO:0000256|RuleBase:RU363075};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU363075};
GN ORFNames=UMAG_06088 {ECO:0000313|EMBL:KIS65998.1};
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS65998.1, ECO:0000313|Proteomes:UP000000561};
RN [1] {ECO:0000313|EMBL:KIS65998.1, ECO:0000313|Proteomes:UP000000561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA Jaffe D.B., Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2] {ECO:0000313|Proteomes:UP000000561}
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003160; KIS65998.1; -; Genomic_DNA.
DR RefSeq; XP_011392447.1; XM_011394145.1.
DR AlphaFoldDB; A0A0D1CG77; -.
DR STRING; 237631.A0A0D1CG77; -.
DR EnsemblFungi; KIS65998; KIS65998; UMAG_06088.
DR GeneID; 23565798; -.
DR KEGG; uma:UMAG_06088; -.
DR VEuPathDB; FungiDB:UMAG_06088; -.
DR eggNOG; KOG2515; Eukaryota.
DR InParanoid; A0A0D1CG77; -.
DR OMA; PRDMHAK; -.
DR OrthoDB; 162888at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000561; Chromosome 21.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; IBA:GO_Central.
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:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
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:UP000000561};
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 244..271
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 291..310
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 356..380
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 406..424
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 436..455
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 476..496
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
SQ SEQUENCE 784 AA; 87777 MW; F38A5696BFDB8A6E CRC64;
MATPPHIPKS QGLRFQQQGN AAYAKASAAK DAAAKDALLS RRNALLQDYA KMHQKPAWSP
SISAAFRFLI IIRVSSAMYS VIKDCDETFG YWEPLHLLVF ARGQHHASVP FQTWEYSPQF
AIRSWAFIAQ YWPLTKSLAY FGVGKRQIFF AVRLLLAFVS SFVDARFYKA VADVFSARVG
RYCLIALATS AGIYEASTAF LPSTFVMHAT TLAFSSCLYP ARLPSSHPSV LSNPSQRPFR
SERLLLAAFS FATGAIIGWP FAIILALPFV IEQLLLRGDD IVANGNYSNW VMSRWSTAIG
AAVLSTILGL PAVAIDTLAY GKLSFVPLNT VLYNLFSRSR GAGPELYGTE PLTYYFSNLL
LNFNVFFLLA LLSLPLMLVT ARLDPKRFQR PMLETKKGHA STEEPSSLFS LALLRIAPFY
LWFILLSVQP HKEERFMYPA YTLLCLNAAV SLYLIRSLAE VGFVQVTKSP YRASKSSVFT
TITSSVLAIA ILLGVLRSVG QLNHYHSPFD VLFHFEGYEL PRVVADVFPE TLSPAIQQRI
ARGLSPVATE QEKEYNDRGY GAENKGVSVD LSIHLTPLST LDKPVRLCYG KEWHRFPTHF
LVPAGVEVEW IQSDFDGILP KHFDVDGASA VEHADAVAHT LETLLGWAWP WSSITRRVQR
GFNDLNQQEM DRYVDVSTCD YLVDLDLPHR SLVSGAESRY EPRYASMSDE WDRVFCGAFL
DAEFSRAVVD PRERLLTTLA RKAGAAMHRA FWLPTSWPGN ANLYGDYCLL RNRQSRFKPA
ASTT
//
