ID A0A0G0WMQ0_9BACT Unreviewed; 357 AA.
AC A0A0G0WMQ0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=GDP-Man:Man(1)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase {ECO:0000256|ARBA:ARBA00032047};
DE EC=2.4.1.132 {ECO:0000256|ARBA:ARBA00012649};
DE EC=2.4.1.257 {ECO:0000256|ARBA:ARBA00011969};
DE AltName: Full=GDP-Man:Man(1)GlcNAc(2)-PP-dolichol mannosyltransferase {ECO:0000256|ARBA:ARBA00032874};
DE AltName: Full=GDP-Man:Man(2)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase {ECO:0000256|ARBA:ARBA00032333};
GN ORFNames=UU67_C0009G0015 {ECO:0000313|EMBL:KKS14044.1};
OS Candidatus Daviesbacteria bacterium GW2011_GWB1_41_5.
OC Bacteria; Candidatus Daviesbacteria.
OX NCBI_TaxID=1618429 {ECO:0000313|EMBL:KKS14044.1, ECO:0000313|Proteomes:UP000034753};
RN [1] {ECO:0000313|EMBL:KKS14044.1, ECO:0000313|Proteomes:UP000034753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- FUNCTION: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and
CC Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol
CC diphosphate. {ECO:0000256|ARBA:ARBA00003142}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC alpha-D-GlcNAc-diphosphodolichol + GDP-alpha-D-mannose = 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 + GDP + H(+); Xref=Rhea:RHEA:29519,
CC Rhea:RHEA-COMP:12624, Rhea:RHEA-COMP:12626, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:132510,
CC ChEBI:CHEBI:132511; EC=2.4.1.257;
CC Evidence={ECO:0000256|ARBA:ARBA00001514};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-(1->3)-beta-D-
CC Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol +
CC GDP + H(+); Xref=Rhea:RHEA:29515, Rhea:RHEA-COMP:11044, Rhea:RHEA-
CC COMP:12624, ChEBI:CHEBI:15378, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:58472, ChEBI:CHEBI:132510; EC=2.4.1.132;
CC Evidence={ECO:0000256|ARBA:ARBA00001253};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
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:KKS14044.1}.
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DR EMBL; LCBN01000009; KKS14044.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0WMQ0; -.
DR PATRIC; fig|1618429.3.peg.281; -.
DR Proteomes; UP000034753; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004378; F:GDP-Man:Man1GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR027054; ALG2.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR028098; Glyco_trans_4-like_N.
DR PANTHER; PTHR45918; ALPHA-1,3/1,6-MANNOSYLTRANSFERASE ALG2; 1.
DR PANTHER; PTHR45918:SF1; ALPHA-1,3_1,6-MANNOSYLTRANSFERASE ALG2; 1.
DR Pfam; PF13439; Glyco_transf_4; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Transferase {ECO:0000313|EMBL:KKS14044.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 17..186
FT /note="Glycosyltransferase subfamily 4-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13439"
FT DOMAIN 198..340
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
SQ SEQUENCE 357 AA; 40926 MW; 4C198BA1F38AEDA9 CRC64;
MSKNLKIALV HDDLVQWGGA EKLLLSLSEV FPRAPIYTSV MDFTNPLIKK YFNSKIIITS
FMQKIPGWRS LYRAFLPLYP LAFEQFDFSA FDIVLSQTTR FAKSIITRPE TKHICYCHTP
PRFLWNFSDE KTPFLLQPYL KFLKQYDRIS SGRVDYWIAG SKNAQERIKQ IYNAESMIIY
PFVDMDKFGY FGGYEGDYLL VISRLNKYKR ADLAILASEK LNIPVKVVGK GPELERLATL
GKQKVELLGT VDDEMLAHLL LGCKAVLVTG EEDFGIVSLE AQALGKPVIA FGKGGALETV
IDGCTGYFFY EQTVESLCDA LEKLYKKGYN QKRCKENAKR FSKERFYNEF QNLILNL
//
