UniProt: C5YEY8

Database: UniProt
Entry: C5YEY8_SORBI

LinkDB:  C5YEY8_SORBI 
Original site:  C5YEY8_SORBI

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Ontology (6)   
   GO (6)   
Chemical reaction (2)   
   KEGG ENZYME (2)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (5)   
   InterPro (3)   
   Pfam (2)   
Literature (2)   
   PubMed (2)   
All databases (19)   

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ID   C5YEY8_SORBI            Unreviewed;       418 AA.
AC   C5YEY8;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Alpha-1,3/1,6-mannosyltransferase ALG2 {ECO:0000256|RuleBase:RU367136};
DE            EC=2.4.1.132 {ECO:0000256|RuleBase:RU367136};
DE            EC=2.4.1.257 {ECO:0000256|RuleBase:RU367136};
DE   AltName: Full=GDP-Man:Man(1)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase {ECO:0000256|RuleBase:RU367136};
GN   ORFNames=SORBI_3006G196300 {ECO:0000313|EMBL:EES11340.1};
OS   Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX   NCBI_TaxID=4558 {ECO:0000313|EMBL:EES11340.1, ECO:0000313|Proteomes:UP000000768};
RN   [1] {ECO:0000313|EMBL:EES11340.1, ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=19189423; DOI=10.1038/nature07723;
RA   Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA   Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA   Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA   Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA   Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA   Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA   Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA   Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT   "The Sorghum bicolor genome and the diversification of grasses.";
RL   Nature 457:551-556(2009).
RN   [2] {ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=29161754; DOI=10.1111/tpj.13781;
RA   McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA   Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA   Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT   "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT   a transcriptome atlas, and signatures of genome organization.";
RL   Plant J. 93:338-354(2018).
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       ECO:0000256|RuleBase:RU367136}.
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         ECO:0000256|RuleBase:RU367136};
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         ECO:0000256|RuleBase:RU367136};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU367136}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU367136}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       {ECO:0000256|RuleBase:RU367136}.
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DR   EMBL; CM000765; EES11340.1; -; Genomic_DNA.
DR   RefSeq; XP_002447012.1; XM_002446967.1.
DR   AlphaFoldDB; C5YEY8; -.
DR   STRING; 4558.C5YEY8; -.
DR   EnsemblPlants; EES11340; EES11340; SORBI_3006G196300.
DR   GeneID; 8060461; -.
DR   Gramene; EES11340; EES11340; SORBI_3006G196300.
DR   KEGG; sbi:8060461; -.
DR   eggNOG; KOG0853; Eukaryota.
DR   HOGENOM; CLU_030619_1_0_1; -.
DR   InParanoid; C5YEY8; -.
DR   OMA; ENVQYHR; -.
DR   OrthoDB; 1377at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000000768; Chromosome 6.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000033; F:alpha-1,3-mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0004378; F:GDP-Man:Man1GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0102704; F:GDP-Man:Man2GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd03805; GT4_ALG2-like; 1.
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   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU367136}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000768};
KW   Transferase {ECO:0000256|RuleBase:RU367136};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          31..191
FT                   /note="Glycosyltransferase subfamily 4-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13439"
FT   DOMAIN          222..390
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
SQ   SEQUENCE   418 AA;  46365 MW;  79CB4F705EE0526B CRC64;
     MAAAGGEVAG ASSGTRTKRL KIAVIHPDLG IGGAERLIVD AACQLAAHGH DVHVFTSHHD
     KNRCFEETVS GLFPVTVYGD FLPRHVFYRF HAVCAYLRCI FVALCVLLRW PFFDVILVDQ
     VSVVIPLLKL RASSKIIFYC HFPDLLLAQH TTMLRKLYRK PIDMIEEITT GMADLILVNS
     KFTAATFART FSCLHARGIE PGVLYPAVSV EQFHEPHAYK LNFLSINRFE RKKNLDLAIS
     AFALLRSVAS TLPGDALQEA TLTVAGGYDK RLKENVEYLE ELKRLAVTEG VSGQVNFVTS
     CSTSERNELL SNCLCVLYTP KDEHFGIVPL EAMAAYKPVI ACNSGGPVET VVNEVTGFLC
     DPSPTEFSKA MLKLVNDHDL AVRLGEQARD HVVQKFSTKT FGDLLNGYVL NVYHERME
//

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