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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)DescriptionActionsGraphical viewLength
Binding sitei107Donor substrate; via carbonyl oxygen1 Publication1
Binding sitei175Donor substrate1 Publication1
Active sitei176Proton donor1
Binding sitei176Acceptor substrate1 Publication1
Binding sitei217Acceptor substrate; via carbonyl oxygen1 Publication1
Binding sitei222Acceptor substrate1 Publication1
Active sitei275Nucleophile1
Binding sitei307Donor substrate1 Publication1

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)DescriptionActionsGraphical viewLength
Mutagenesisi62Q → A: Slightly reduces catalytic activity. 1 Publication1
Mutagenesisi107Y → F or Q: Slightly reduces catalytic activity. 1 Publication1
Mutagenesisi132D → N: Slightly reduces catalytic activity. 1 Publication1
Mutagenesisi175N → A: Abolishes catalytic activity. 1 Publication1
Mutagenesisi176E → Q: Abolishes catalytic activity. 1 Publication1
Mutagenesisi244Y → F or Q: Moderately reduces hydrolysis, and causes a 10-fold reduction in transglycosylation activity. 1 Publication1
Mutagenesisi275E → Q: Abolishes catalytic activity. 1 Publication1
Mutagenesisi307Y → Q: Moderately reduces catalytic activity. 1 Publication1
Mutagenesisi404F → A: Slightly reduces catalytic activity. 1 Publication1
Mutagenesisi474Y → A: No effect. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
ChainiPRO_000001047525 – 5311,3-beta-glucanosyltransferase GAS2Add BLAST507
PropeptideiPRO_0000010476532 – 555Removed in mature formSequence analysisAdd BLAST24

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Glycosylationi498N-linked (GlcNAc...)Sequence analysis1
Lipidationi531GPI-anchor amidated aspartateSequence analysis1

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 interactors.
DIPiDIP-4669N.
IntActiQ06135. 3 interactors.
MINTiMINT-526782.

Structurei

Secondary structure

1555
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi36 – 39Combined sources4
Beta strandi42 – 45Combined sources4
Turni46 – 48Combined sources3
Beta strandi54 – 58Combined sources5
Turni72 – 75Combined sources4
Helixi82 – 84Combined sources3
Helixi86 – 99Combined sources14
Beta strandi102 – 106Combined sources5
Helixi116 – 124Combined sources9
Beta strandi128 – 133Combined sources6
Beta strandi142 – 144Combined sources3
Helixi149 – 162Combined sources14
Beta strandi168 – 178Combined sources11
Helixi184 – 186Combined sources3
Helixi187 – 203Combined sources17
Beta strandi204 – 206Combined sources3
Beta strandi211 – 215Combined sources5
Turni219 – 221Combined sources3
Helixi222 – 228Combined sources7
Beta strandi239 – 243Combined sources5
Helixi252 – 255Combined sources4
Helixi257 – 264Combined sources8
Beta strandi271 – 276Combined sources6
Beta strandi280 – 283Combined sources4
Helixi288 – 292Combined sources5
Helixi295 – 298Combined sources4
Beta strandi303 – 307Combined sources5
Beta strandi313 – 315Combined sources3
Beta strandi318 – 321Combined sources4
Beta strandi327 – 329Combined sources3
Helixi331 – 342Combined sources12
Helixi350 – 354Combined sources5
Turni372 – 374Combined sources3
Helixi387 – 396Combined sources10
Beta strandi398 – 401Combined sources4
Helixi408 – 410Combined sources3
Helixi411 – 418Combined sources8
Turni419 – 421Combined sources3
Helixi424 – 427Combined sources4
Turni431 – 434Combined sources4
Turni438 – 441Combined sources4
Helixi444 – 459Combined sources16
Beta strandi473 – 475Combined sources3
Helixi477 – 480Combined sources4
Helixi490 – 501Combined sources12

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ06135.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni134 – 142Donor substrate binding1 Publication9

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2W61X-ray1.62A1-555[»]
2W62X-ray1.85A1-555[»]
2W63X-ray1.90A1-555[»]
5FIHX-ray1.80A1-555[»]
ProteinModelPortaliQ06135.
SMRiQ06135.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31605. 34 interactors.
DIPiDIP-4669N.
IntActiQ06135. 3 interactors.
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: November 2, 2016
This is version 120 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.