G3J3K0 · FKS1_CORMM
- Protein1,3-beta-glucan synthase component
- GeneGLS1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1946 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytic subunit of the 1,3-beta-glucan synthase (GS) (PubMed:35816703).
Synthesizes 1,3-beta-glucan, a major structural component of the fungal cell wall (PubMed:35816703).
Involved in cell wall synthesis, maintenance and remodeling (By similarity).
Synthesizes 1,3-beta-glucan, a major structural component of the fungal cell wall (PubMed:35816703).
Involved in cell wall synthesis, maintenance and remodeling (By similarity).
Catalytic activity
- [(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-beta-D-glucosyl](n+1) + H+ + UDP
[(1→3)-β-D-glucosyl](n) RHEA-COMP:11146 + CHEBI:58885 = [(1→3)-β-D-glucosyl](n+1) RHEA-COMP:14303 + CHEBI:15378 + CHEBI:58223
Activity regulation
Activated by iron ions (PubMed:35816703).
Inhibited by manganese, copper and zinc ions (PubMed:35816703).
Inhibited by manganese, copper and zinc ions (PubMed:35816703).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
84.3 μM | UDP-glucose | 7 | 37 |
kcat is 1.42 min-1 for UDP-glucose (at 37 degrees Celsius and pH 7).
pH Dependence
Optimum pH is 7.
Temperature Dependence
Optimum temperature is 37 degrees Celsius.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | 1,3-beta-D-glucan synthase complex | |
Molecular Function | 1,3-beta-D-glucan synthase activity | |
Biological Process | (1->3)-beta-D-glucan biosynthetic process | |
Biological Process | cell wall organization | |
Biological Process | fungal-type cell wall polysaccharide biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name1,3-beta-glucan synthase component
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Cordycipitaceae > Cordyceps
Accessions
- Primary accessionG3J3K0
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Cell membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 489-509 | Helical | ||||
Sequence: WFHLLLNFNRIWVIHLTMFWF | ||||||
Transmembrane | 537-557 | Helical | ||||
Sequence: FSIVGFGGAIASLIQIFATLA | ||||||
Transmembrane | 576-596 | Helical | ||||
Sequence: LLFLIVILVLNVAPGVKVFMF | ||||||
Transmembrane | 618-638 | Helical | ||||
Sequence: IGIVHFVIAVFTFLFFSVMPL | ||||||
Transmembrane | 675-695 | Helical | ||||
Sequence: FGLWLTVFGAKFGESYVYLTL | ||||||
Transmembrane | 734-754 | Helical | ||||
Sequence: IVLILMTFTDLIFFFLDTYLF | ||||||
Transmembrane | 1356-1376 | Helical | ||||
Sequence: NMFIMLSVQSFMLTLMSIGAL | ||||||
Transmembrane | 1413-1433 | Helical | ||||
Sequence: CIISIFFVFFISFVPLIVQEL | ||||||
Transmembrane | 1500-1520 | Helical | ||||
Sequence: FAGQSIYFGARLLMMLLFATS | ||||||
Transmembrane | 1523-1543 | Helical | ||||
Sequence: WQPALTYFWIVLLGLIISPFL | ||||||
Transmembrane | 1615-1635 | Helical | ||||
Sequence: IFLTEILTPLLLAATTTVAYL | ||||||
Transmembrane | 1667-1687 | Helical | ||||
Sequence: LAVVAFAPIGINAGVLAAMFG | ||||||
Transmembrane | 1703-1723 | Helical | ||||
Sequence: FGPVLAGIAHGAAAVFMIIFF | ||||||
Transmembrane | 1738-1758 | Helical | ||||
Sequence: LAGIIAAMCIQRFIFKLIVSL | ||||||
Transmembrane | 1803-1823 | Helical | ||||
Sequence: FSADFILGHWILFMMAPLILI | ||||||
Transmembrane | 1864-1884 | Helical | ||||
Sequence: AILYFVLFIIFLALVVAPGVI |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000456875 | 1-1946 | 1,3-beta-glucan synthase component | |||
Sequence: MSGYQGGHHDQYDQGYGQAGHGDGYYQDDQYYDQGHGDHAAQGDHAAQGDHGAQGTQGDGYYDESGYYHADANNPYHQDGGYYDGHDQYQDDYYNNNQGYYDGEYNQGYAQGGRHPSEEESETFSDFTMRSDMARAAEMDYYGRGDEQYNGYGEGGRGYRPPSSQLSYGGNRSSGASTPNYGMEYGNGLASQRSKEPYPAWTSDAQIPLSKEEIEDIFLDLTSKFGFQRDSMRNMYDHLMTLLDSRASRMTPNQALLSLHADYIGGDNANYRKWYFAAHLDLDDAVGFANASTKNRKRKAKKGKKKGGEAGNEAETLQELEGDDSLEAAEYRWKTRMNRMSQYDRVRQIALYLLCWGEANQVRFMPECLCFIFKCADDYLNSPACQALVEPVEEFTFLNNVITPLYQYCRDQGYEILNGVYVRRERDHKHIIGYDDCNQLFWYPEGIERIVLEDKSKLVDLPPAERYLKLKEVNWKKCFFKTYKESRSWFHLLLNFNRIWVIHLTMFWFYTSHNAPSLITYQYEQQKDNQPPASKQFSIVGFGGAIASLIQIFATLAEWVYVPRRWAGAQHLTKRLLFLIVILVLNVAPGVKVFMFHGNKDGKDADQKNKDTPIDKAIGIVHFVIAVFTFLFFSVMPLGGLLGSYLTKKSRRYVASQTFTASYPRLTGNDMAMSFGLWLTVFGAKFGESYVYLTLSFRDPIRYLSIMKIDCLGDAMFGSTAATQQILCKHQPTIVLILMTFTDLIFFFLDTYLFYVILNTVFSIARSFYIGSSIWTPWRNIFSRLPKRIYSKVLATTDMEIKYKPKVLISQVWNAIVISMYREHLLAIDHVQKLLYHQVPSEQEGKRTLRAPTFFVSQEDHSFKTEFFPSHSEAERRISFFAQSLSTPIPEPVPVDNMPTFTVMIPHYSEKILLSLREIIREDEPYSRVTLLEYLKQLHPHEWECFVKDTKILADETAQMNGEPEKSEKDTAKSKIDDLPFYCIGFKSSAPEYTLRTRIWASLRSQTLYRTVSGFMNYSRAIKLLYRVENPEVVQMFGGNSEKLERELERMARRKFKLVVSMQRYSKFKKEEMENAEFLLRAYPDLQIAYLDEEPPLAEGEEPRLYSALIDGHSELMENGMRRPKFRVQLSGNPVLGDGKSDNQNHAIIFYRGEYIQLIDANQDNYLEECLKIRSVLAEFEEMKPDNHSPYTPGVKNDVHTPVAILGAREYIFSENIGILGDVAAGKEQTFGTLFARTMAQVGGKLHYGHPDFLNGIFMTTRGGVSKAQKGLHLNEDIFAGMNALVRGGRIKHCEYYQCGKGRDLGFGSILNFTTKIGTGMGEQWLSREYYYLGTQLPLDRFLSFYYAHAGFHVNNMFIMLSVQSFMLTLMSIGALRHETIRCDYNPQKPITDPLYPTKCSNTDELMGWVYRCIISIFFVFFISFVPLIVQELTERGVWRAALRFIKQFCSLSPFFEVFVCQIYANSVQSDLAFGGARYIGTGRGFATARIPFGVLYSRFAGQSIYFGARLLMMLLFATSTAWQPALTYFWIVLLGLIISPFLYNPHQFAWTDFFIDYRDFLRWLSRGNSRAHASSWIMFCRLSRTRITGYKRKVMGDASAKMSADVPRAAVANIFLTEILTPLLLAATTTVAYLFVNAQTGVTDNDKNSSSSPGFKIGPSGALIRLAVVAFAPIGINAGVLAAMFGMACCMGPVLNMCCKKFGPVLAGIAHGAAAVFMIIFFEVMYVLEGFNFARALAGIIAAMCIQRFIFKLIVSLALTREFKTDQSNIAFWNGKWYSMGWHSVSQPAREFLCKITELSMFSADFILGHWILFMMAPLILIPQIDKIHSMMLFWLLPSRQIRPPIYSMKQSKLRRRRVIRFAILYFVLFIIFLALVVAPGVIGKKFLGDTIFKALDNGNGGPANLHLLQPWGLDNNNTEGKTETGTKAGGADASATDASKLRLF | ||||||
Glycosylation | 171 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 290 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1017 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1312 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1649 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1918 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Expression
Developmental stage
Expressed in mycelia (at protein level).
Interaction
Subunit
Component of the 1,3-beta-glucan synthase (GS) complex composed of a catalytic subunit GLS1 and a regulatory subunit RHO1.
Protein-protein interaction databases
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-127 | Disordered | ||||
Sequence: MSGYQGGHHDQYDQGYGQAGHGDGYYQDDQYYDQGHGDHAAQGDHAAQGDHGAQGTQGDGYYDESGYYHADANNPYHQDGGYYDGHDQYQDDYYNNNQGYYDGEYNQGYAQGGRHPSEEESETFSDF | ||||||
Compositional bias | 90-104 | Polar residues | ||||
Sequence: QDDYYNNNQGYYDGE | ||||||
Region | 152-198 | Disordered | ||||
Sequence: YGEGGRGYRPPSSQLSYGGNRSSGASTPNYGMEYGNGLASQRSKEPY | ||||||
Compositional bias | 164-187 | Polar residues | ||||
Sequence: SQLSYGGNRSSGASTPNYGMEYGN | ||||||
Region | 297-316 | Disordered | ||||
Sequence: KRKAKKGKKKGGEAGNEAET | ||||||
Region | 1920-1946 | Disordered | ||||
Sequence: TEGKTETGTKAGGADASATDASKLRLF |
Sequence similarities
Belongs to the glycosyltransferase 48 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,946
- Mass (Da)221,664
- Last updated2022-12-14 v2
- Checksum1F5848636FE92160
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 90-104 | Polar residues | ||||
Sequence: QDDYYNNNQGYYDGE | ||||||
Compositional bias | 164-187 | Polar residues | ||||
Sequence: SQLSYGGNRSSGASTPNYGMEYGN |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JH126399 EMBL· GenBank· DDBJ | EGX96528.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation |