ID A0A0G0NJD5_9BACT Unreviewed; 393 AA.
AC A0A0G0NJD5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=UT44_C0017G0016 {ECO:0000313|EMBL:KKR16224.1};
OS Candidatus Levybacteria bacterium GW2011_GWA1_39_32.
OC Bacteria; Candidatus Levybacteria.
OX NCBI_TaxID=1618454 {ECO:0000313|EMBL:KKR16224.1, ECO:0000313|Proteomes:UP000034624};
RN [1] {ECO:0000313|EMBL:KKR16224.1, ECO:0000313|Proteomes:UP000034624}
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:KKR16224.1}.
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DR EMBL; LBWU01000017; KKR16224.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0NJD5; -.
DR PATRIC; fig|1618454.3.peg.379; -.
DR Proteomes; UP000034624; 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 Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 14..199
FT /note="Glycosyltransferase subfamily 4-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13439"
FT DOMAIN 222..362
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
SQ SEQUENCE 393 AA; 44797 MW; 753AA4B608304E06 CRC64;
MLKVAIVHDY IKEYGGAERV LESLHSVFPD APVYTSVYLP KYLGPHRKRF VNWNIKTSWA
DVLPFRAKLI SPIRLIAPTL FRSLDLSKFD VVIVSATGAY SPNTITTRSY KDSKKKAVHI
SYVHTPPRYL YGYETARNWK KNVLTRALGM LAIHWLRMVD FRSSQNVDHF IANSEETKKR
IKKFYKKDAT VIYPPVDISS KYQVVSIKGE NTKYRMHNTG YYLAGGRIAR AKHPELIIKA
FLQNGLPLKV FGKSFGGYES ELKSKIKNKI SKIDFLGEVT DEEKDRLMVG AKAFVFASQD
EDFGIIPVEA MMAGTPVIAH RSGGVLETVI DGKTGLFFDE LSSESINKAV KRFETLRQAQ
GKFDSDEIKQ HAQKFSKARF EKEIKEFVES EMK
//
