BMT3_KOMPC
ID BMT3_KOMPC Reviewed; 594 AA.
AC F2QQ67;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Beta-mannosyltransferase 3;
DE EC=2.4.1.-;
GN Name=BMT3; OrderedLocusNames=PP7435_Chr1-1431;
OS Komagataella phaffii (strain ATCC 76273 / CBS 7435 / CECT 11047 / NRRL
OS Y-11430 / Wegner 21-1) (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=981350;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76273 / CBS 7435 / CECT 11047 / NRRL Y-11430 / Wegner 21-1;
RX PubMed=21575661; DOI=10.1016/j.jbiotec.2011.04.014;
RA Kueberl A., Schneider J., Thallinger G.G., Anderl I., Wibberg D., Hajek T.,
RA Jaenicke S., Brinkrolf K., Goesmann A., Szczepanowski R., Puehler A.,
RA Schwab H., Glieder A., Pichler H.;
RT "High-quality genome sequence of Pichia pastoris CBS7435.";
RL J. Biotechnol. 154:312-320(2011).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 76273 / CBS 7435 / CECT 11047 / NRRL Y-11430 / Wegner 21-1;
RX PubMed=27388471; DOI=10.1093/femsyr/fow051;
RA Valli M., Tatto N.E., Peymann A., Gruber C., Landes N., Ekker H.,
RA Thallinger G.G., Mattanovich D., Gasser B., Graf A.B.;
RT "Curation of the genome annotation of Pichia pastoris (Komagataella
RT phaffii) CBS7435 from gene level to protein function.";
RL FEMS Yeast Res. 16:0-0(2016).
CC -!- FUNCTION: Beta-mannosyltransferase involved in cell wall biosynthesis.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the BMT family. {ECO:0000305}.
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DR EMBL; FR839628; CCA37545.1; -; Genomic_DNA.
DR AlphaFoldDB; F2QQ67; -.
DR CAZy; GT91; Glycosyltransferase Family 91.
DR EnsemblFungi; CCA37545; CCA37545; PP7435_CHR1-1431.
DR HOGENOM; CLU_013841_3_0_1; -.
DR Proteomes; UP000006853; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000030; F:mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR InterPro; IPR021988; BMT1.
DR PANTHER; PTHR37989; PTHR37989; 2.
DR Pfam; PF12141; DUF3589; 2.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Coiled coil; Glycoprotein;
KW Glycosyltransferase; Membrane; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..594
FT /note="Beta-mannosyltransferase 3"
FT /id="PRO_0000426103"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..594
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 517..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 512..594
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 594 AA; 68423 MW; DB09B57D918FEB1A CRC64;
MRIRSNVLLL STAGALALVW FAVVFSWDDK SIFGIPTPGH AVASAYDSSV TLGTFNDMEV
DSYVTNIYDN APVLGCYDLS YHGLLKVSPK HEILCDMKFI RARVLETEAY AALKDLEHKK
LTEEEKIEKH WFTFYGSSVF LPDHDVHYLV RRVVFSGEGK ANRPITSILV AQIYDKNWNE
LNGHFLNVLN PNTGKLQHHA FPQVLPIAVN WDRNSKYRGQ EDPRVVLRRG RFGPDPLVMF
NTLTQNNKLR RLFTISPFDQ YKTVMYRTNA FKMQTTEKNW VPFFLKDDQE SVHFVYSFNP
LRVLNCSLDN GACDVLFELP HDFGMSSELR GATPMLNLPQ AIPMADDKEI WVSFPRTRIS
DCGCSETMYR PMLMLFVREG TNFFAELLSS SIDFGLEVIP YTGDGLPCSS GQSVLIPNSI
DNWEVTGSNG EDILSLTFSE ADKSTSVVHI RGLYKYLSEL DGYGGPEAED EHNFQRILSD
LHFDGKKTIE NFKKVQSCAL DAAKAYCKEY GVTRGEEDRL KNKEKERKIE EKRKKEEERK
KKEEEKKKKE EEEKKKKEEE EEEEKRLKEL KKKLKELQEE LEKQKDEVKD TKAK