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Protein

1,3-beta-glucanosyltransferase GAS2

Gene

GAS2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in spore wall assembly.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei107 – 1071Donor substrate; via carbonyl oxygen1 Publication
Binding sitei175 – 1751Donor substrate1 Publication
Active sitei176 – 1761Proton donor
Binding sitei176 – 1761Acceptor substrate1 Publication
Binding sitei217 – 2171Acceptor substrate; via carbonyl oxygen1 Publication
Binding sitei222 – 2221Acceptor substrate1 Publication
Active sitei275 – 2751Nucleophile
Binding sitei307 – 3071Donor substrate1 Publication

GO - Molecular functioni

  • 1,3-beta-glucanosyltransferase activity Source: SGD

GO - Biological processi

  • ascospore wall assembly Source: SGD
  • fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

BioCyciYEAST:G3O-32419-MONOMER.

Protein family/group databases

CAZyiCBM43. Carbohydrate-Binding Module Family 43.
GH72. Glycoside Hydrolase Family 72.

Names & Taxonomyi

Protein namesi
Recommended name:
1,3-beta-glucanosyltransferase GAS2 (EC:2.4.1.-1 Publication)
Alternative name(s):
Glycolipid-anchored surface protein 2
Gene namesi
Name:GAS2
Ordered Locus Names:YLR343W
ORF Names:L8300.5
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR343W.
SGDiS000004335. GAS2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi62 – 621Q → A: Slightly reduces catalytic activity. 1 Publication
Mutagenesisi107 – 1071Y → F or Q: Slightly reduces catalytic activity. 1 Publication
Mutagenesisi132 – 1321D → N: Slightly reduces catalytic activity. 1 Publication
Mutagenesisi175 – 1751N → A: Abolishes catalytic activity. 1 Publication
Mutagenesisi176 – 1761E → Q: Abolishes catalytic activity. 1 Publication
Mutagenesisi244 – 2441Y → F or Q: Moderately reduces hydrolysis, and causes a 10-fold reduction in transglycosylation activity. 1 Publication
Mutagenesisi275 – 2751E → Q: Abolishes catalytic activity. 1 Publication
Mutagenesisi307 – 3071Y → Q: Moderately reduces catalytic activity. 1 Publication
Mutagenesisi404 – 4041F → A: Slightly reduces catalytic activity. 1 Publication
Mutagenesisi474 – 4741Y → A: No effect. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence analysisAdd
BLAST
Chaini25 – 5315071,3-beta-glucanosyltransferase GAS2PRO_0000010475Add
BLAST
Propeptidei532 – 55524Removed in mature formSequence analysisPRO_0000010476Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi89 ↔ 1182 Publications
Disulfide bondi231 ↔ 3672 Publications
Disulfide bondi247 ↔ 2782 Publications
Disulfide bondi390 ↔ 4422 Publications
Disulfide bondi392 ↔ 4892 Publications
Disulfide bondi399 ↔ 4662 Publications
Disulfide bondi419 ↔ 4242 Publications
Glycosylationi498 – 4981N-linked (GlcNAc...)Sequence analysis
Lipidationi531 – 5311GPI-anchor amidated aspartateSequence analysis

Post-translational modificationi

N-glycosylated.

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

PTM databases

iPTMnetiQ06135.

Expressioni

Developmental stagei

Expressed exclusively during sporulation (at protein level).1 Publication

Interactioni

Protein-protein interaction databases

BioGridi31605. 34 interactions.
DIPiDIP-4669N.
IntActiQ06135. 3 interactions.
MINTiMINT-526782.

Structurei

Secondary structure

1
555
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi36 – 394Combined sources
Beta strandi42 – 454Combined sources
Turni46 – 483Combined sources
Beta strandi54 – 585Combined sources
Turni72 – 754Combined sources
Helixi82 – 843Combined sources
Helixi86 – 9914Combined sources
Beta strandi102 – 1065Combined sources
Helixi116 – 1249Combined sources
Beta strandi128 – 1336Combined sources
Beta strandi142 – 1443Combined sources
Helixi149 – 16214Combined sources
Beta strandi168 – 17811Combined sources
Helixi184 – 1863Combined sources
Helixi187 – 20317Combined sources
Beta strandi204 – 2063Combined sources
Beta strandi211 – 2155Combined sources
Turni219 – 2213Combined sources
Helixi222 – 2287Combined sources
Beta strandi239 – 2435Combined sources
Helixi252 – 2554Combined sources
Helixi257 – 2648Combined sources
Beta strandi271 – 2766Combined sources
Beta strandi280 – 2834Combined sources
Helixi288 – 2925Combined sources
Helixi295 – 2984Combined sources
Beta strandi303 – 3075Combined sources
Beta strandi313 – 3153Combined sources
Beta strandi318 – 3214Combined sources
Beta strandi327 – 3293Combined sources
Helixi331 – 34212Combined sources
Helixi350 – 3545Combined sources
Turni372 – 3743Combined sources
Helixi387 – 39610Combined sources
Beta strandi398 – 4014Combined sources
Helixi408 – 4103Combined sources
Helixi411 – 4188Combined sources
Turni419 – 4213Combined sources
Helixi424 – 4274Combined sources
Turni431 – 4344Combined sources
Turni438 – 4414Combined sources
Helixi444 – 45916Combined sources
Beta strandi473 – 4753Combined sources
Helixi477 – 4804Combined sources
Helixi490 – 50112Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2W61X-ray1.62A1-555[»]
2W62X-ray1.85A1-555[»]
2W63X-ray1.90A1-555[»]
5FIHX-ray1.80A1-555[»]
ProteinModelPortaliQ06135.
SMRiQ06135. Positions 27-506.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06135.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni134 – 1429Donor substrate binding1 Publication

Sequence similaritiesi

Belongs to the glycosyl hydrolase 72 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

GeneTreeiENSGT00390000011003.
HOGENOMiHOG000164982.
InParanoidiQ06135.
OMAiEWCGYST.
OrthoDBiEOG092C1TYR.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR004886. Glucanosyltransferase.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR012946. X8.
[Graphical view]
PfamiPF03198. Glyco_hydro_72. 1 hit.
PF07983. X8. 1 hit.
[Graphical view]
SMARTiSM00768. X8. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q06135-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKKQNFYAA IIVAIFLCLQ LSHGSSGVSF EKTPAIKIVG NKFFDSESGE
60 70 80 90 100
QFFIKGIAYQ LQRSEEELSN ANGAFETSYI DALADPKICL RDIPFLKMLG
110 120 130 140 150
VNTLRVYAID PTKSHDICME ALSAEGMYVL LDLSEPDISI NRENPSWDVH
160 170 180 190 200
IFERYKSVID AMSSFPNLLG YFAGNEVTND HTNTFASPFV KAAIRDAKEY
210 220 230 240 250
ISHSNHRKIP VGYSTNDDAM TRDNLARYFV CGDVKADFYG INMYEWCGYS
260 270 280 290 300
TYGTSGYRER TKEFEGYPIP VFFSEFGCNL VRPRPFTEVS ALYGNKMSSV
310 320 330 340 350
WSGGLAYMYF EEENEYGVVK INDNDGVDIL PDFKNLKKEF AKADPKGITE
360 370 380 390 400
EEYLTAKEPT EVESVECPHI AVGVWEANEK LPETPDRSKC ACLDEILPCE
410 420 430 440 450
IVPFGAESGK YEEYFSYLCS KVDCSDILAN GKTGEYGEFS DCSVEQKLSL
460 470 480 490 500
QLSKLYCKIG ANDRHCPLND KNVYFNLESL QPLTSESICK NVFDSIRNIT
510 520 530 540 550
YNHGDYSKSN PSRSKESLNV KYPSSEEREN DGTIAFKTSG FVILLISMIA

AGILL
Length:555
Mass (Da):62,362
Last modified:November 1, 1997 - v1
Checksum:i15395E4F137DAC7F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19028 Genomic DNA. Translation: AAB67255.1.
BK006945 Genomic DNA. Translation: DAA09648.1.
PIRiS51346.
RefSeqiNP_013447.1. NM_001182232.1.

Genome annotation databases

EnsemblFungiiYLR343W; YLR343W; YLR343W.
GeneIDi851056.
KEGGisce:YLR343W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19028 Genomic DNA. Translation: AAB67255.1.
BK006945 Genomic DNA. Translation: DAA09648.1.
PIRiS51346.
RefSeqiNP_013447.1. NM_001182232.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2W61X-ray1.62A1-555[»]
2W62X-ray1.85A1-555[»]
2W63X-ray1.90A1-555[»]
5FIHX-ray1.80A1-555[»]
ProteinModelPortaliQ06135.
SMRiQ06135. Positions 27-506.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31605. 34 interactions.
DIPiDIP-4669N.
IntActiQ06135. 3 interactions.
MINTiMINT-526782.

Protein family/group databases

CAZyiCBM43. Carbohydrate-Binding Module Family 43.
GH72. Glycoside Hydrolase Family 72.

PTM databases

iPTMnetiQ06135.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR343W; YLR343W; YLR343W.
GeneIDi851056.
KEGGisce:YLR343W.

Organism-specific databases

EuPathDBiFungiDB:YLR343W.
SGDiS000004335. GAS2.

Phylogenomic databases

GeneTreeiENSGT00390000011003.
HOGENOMiHOG000164982.
InParanoidiQ06135.
OMAiEWCGYST.
OrthoDBiEOG092C1TYR.

Enzyme and pathway databases

BioCyciYEAST:G3O-32419-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ06135.
PROiQ06135.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR004886. Glucanosyltransferase.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR012946. X8.
[Graphical view]
PfamiPF03198. Glyco_hydro_72. 1 hit.
PF07983. X8. 1 hit.
[Graphical view]
SMARTiSM00768. X8. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGAS2_YEAST
AccessioniPrimary (citable) accession number: Q06135
Secondary accession number(s): D6VYY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 7, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.