GAS2_YEAST
ID GAS2_YEAST Reviewed; 555 AA.
AC Q06135; D6VYY2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=1,3-beta-glucanosyltransferase GAS2;
DE EC=2.4.1.- {ECO:0000269|PubMed:19097997};
DE AltName: Full=Glycolipid-anchored surface protein 2;
DE Flags: Precursor;
GN Name=GAS2; OrderedLocusNames=YLR343W; ORFNames=L8300.5;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=17189486; DOI=10.1128/ec.00321-06;
RA Ragni E., Coluccio A., Rolli E., Rodriguez-Pena J.M., Colasante G.,
RA Arroyo J., Neiman A.M., Popolo L.;
RT "GAS2 and GAS4, a pair of developmentally regulated genes required for
RT spore wall assembly in Saccharomyces cerevisiae.";
RL Eukaryot. Cell 6:302-316(2007).
RN [4]
RP FUNCTION.
RX PubMed=17397106; DOI=10.1002/yea.1473;
RA Ragni E., Fontaine T., Gissi C., Latge J.-P., Popolo L.;
RT "The Gas family of proteins of Saccharomyces cerevisiae: characterization
RT and evolutionary analysis.";
RL Yeast 24:297-308(2007).
RN [5]
RP DISULFIDE BONDS.
RX PubMed=18468997; DOI=10.1074/jbc.m801562200;
RA Popolo L., Ragni E., Carotti C., Palomares O., Aardema R., Back J.W.,
RA Dekker H.L., de Koning L.J., de Jong L., de Koster C.G.;
RT "Disulfide bond structure and domain organization of yeast beta(1,3)-
RT glucanosyltransferases involved in cell wall biogenesis.";
RL J. Biol. Chem. 283:18553-18565(2008).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) OF WILD-TYPE AND MUTANT GLN-176 IN
RP COMPLEX WITH SUBSTRATE ANALOGS, FUNCTION, CATALYTIC ACTIVITY, DISULFIDE
RP BONDS, AND MUTAGENESIS OF GLN-62; TYR-107; ASP-132; ASN-175; GLU-176;
RP TYR-244; GLU-275; TYR-307; PHE-404 AND TYR-474.
RX PubMed=19097997; DOI=10.1074/jbc.m807990200;
RA Hurtado-Guerrero R., Schuettelkopf A.W., Mouyna I., Ibrahim A.F.M.,
RA Shepherd S., Fontaine T., Latge J.-P., van Aalten D.M.F.;
RT "Molecular mechanisms of yeast cell wall glucan remodeling.";
RL J. Biol. Chem. 284:8461-8469(2009).
CC -!- FUNCTION: Splits internally a 1,3-beta-glucan molecule and transfers
CC the newly generated reducing end (the donor) to the non-reducing end of
CC another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta
CC linkage, resulting in the elongation of 1,3-beta-glucan chains in the
CC cell wall. Involved in spore wall assembly.
CC {ECO:0000269|PubMed:17189486, ECO:0000269|PubMed:17397106,
CC ECO:0000269|PubMed:19097997}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed exclusively during sporulation (at
CC protein level). {ECO:0000269|PubMed:17189486}.
CC -!- PTM: N-glycosylated.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family. {ECO:0000305}.
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DR EMBL; U19028; AAB67255.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09648.1; -; Genomic_DNA.
DR PIR; S51346; S51346.
DR RefSeq; NP_013447.1; NM_001182232.1.
DR PDB; 2W61; X-ray; 1.62 A; A=1-555.
DR PDB; 2W62; X-ray; 1.85 A; A=1-555.
DR PDB; 2W63; X-ray; 1.90 A; A=1-555.
DR PDB; 5FIH; X-ray; 1.80 A; A=1-555.
DR PDB; 5O9O; X-ray; 1.90 A; A=1-555.
DR PDB; 5O9P; X-ray; 1.75 A; A=1-555.
DR PDB; 5O9Q; X-ray; 1.40 A; A=1-555.
DR PDB; 5O9R; X-ray; 1.70 A; A=1-555.
DR PDB; 5O9Y; X-ray; 1.57 A; A=1-555.
DR PDB; 5OA2; X-ray; 2.15 A; A/B/C=1-555.
DR PDB; 5OA6; X-ray; 1.94 A; A=1-555.
DR PDBsum; 2W61; -.
DR PDBsum; 2W62; -.
DR PDBsum; 2W63; -.
DR PDBsum; 5FIH; -.
DR PDBsum; 5O9O; -.
DR PDBsum; 5O9P; -.
DR PDBsum; 5O9Q; -.
DR PDBsum; 5O9R; -.
DR PDBsum; 5O9Y; -.
DR PDBsum; 5OA2; -.
DR PDBsum; 5OA6; -.
DR AlphaFoldDB; Q06135; -.
DR SMR; Q06135; -.
DR BioGRID; 31605; 72.
DR DIP; DIP-4669N; -.
DR IntAct; Q06135; 3.
DR MINT; Q06135; -.
DR STRING; 4932.YLR343W; -.
DR CAZy; CBM43; Carbohydrate-Binding Module Family 43.
DR CAZy; GH72; Glycoside Hydrolase Family 72.
DR iPTMnet; Q06135; -.
DR PaxDb; Q06135; -.
DR PRIDE; Q06135; -.
DR EnsemblFungi; YLR343W_mRNA; YLR343W; YLR343W.
DR GeneID; 851056; -.
DR KEGG; sce:YLR343W; -.
DR SGD; S000004335; GAS2.
DR VEuPathDB; FungiDB:YLR343W; -.
DR eggNOG; ENOG502QRZZ; Eukaryota.
DR GeneTree; ENSGT00940000176308; -.
DR HOGENOM; CLU_021855_2_0_1; -.
DR InParanoid; Q06135; -.
DR OMA; ICLRDIP; -.
DR BioCyc; YEAST:G3O-32419-MON; -.
DR EvolutionaryTrace; Q06135; -.
DR PRO; PR:Q06135; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06135; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; IDA:SGD.
DR GO; GO:0030476; P:ascospore wall assembly; IMP:SGD.
DR GO; GO:0034411; P:cell wall (1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
DR GO; GO:0071970; P:fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
DR InterPro; IPR004886; Glucanosyltransferase.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR012946; X8.
DR PANTHER; PTHR31468; PTHR31468; 1.
DR Pfam; PF03198; Glyco_hydro_72; 1.
DR Pfam; PF07983; X8; 1.
DR SMART; SM00768; X8; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell wall biogenesis/degradation;
KW Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Reference proteome; Signal; Transferase.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..531
FT /note="1,3-beta-glucanosyltransferase GAS2"
FT /id="PRO_0000010475"
FT PROPEP 532..555
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010476"
FT ACT_SITE 176
FT /note="Proton donor"
FT ACT_SITE 275
FT /note="Nucleophile"
FT BINDING 107
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="1"
FT /ligand_note="donor substrate"
FT /evidence="ECO:0000305|PubMed:19097997"
FT BINDING 134..142
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="1"
FT /ligand_note="donor substrate"
FT /evidence="ECO:0000305|PubMed:19097997"
FT BINDING 175
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="1"
FT /ligand_note="donor substrate"
FT /evidence="ECO:0000305|PubMed:19097997"
FT BINDING 176
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="2"
FT /ligand_note="acceptor substrate"
FT /evidence="ECO:0000305|PubMed:19097997"
FT BINDING 217
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="2"
FT /ligand_note="acceptor substrate"
FT /evidence="ECO:0000305|PubMed:19097997"
FT BINDING 222
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="2"
FT /ligand_note="acceptor substrate"
FT /evidence="ECO:0000305|PubMed:19097997"
FT BINDING 307
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="1"
FT /ligand_note="donor substrate"
FT /evidence="ECO:0000305|PubMed:19097997"
FT LIPID 531
FT /note="GPI-anchor amidated aspartate"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 89..118
FT /evidence="ECO:0000269|PubMed:18468997,
FT ECO:0000269|PubMed:19097997"
FT DISULFID 231..367
FT /evidence="ECO:0000269|PubMed:18468997,
FT ECO:0000269|PubMed:19097997"
FT DISULFID 247..278
FT /evidence="ECO:0000269|PubMed:18468997,
FT ECO:0000269|PubMed:19097997"
FT DISULFID 390..442
FT /evidence="ECO:0000269|PubMed:18468997,
FT ECO:0000269|PubMed:19097997"
FT DISULFID 392..489
FT /evidence="ECO:0000269|PubMed:18468997,
FT ECO:0000269|PubMed:19097997"
FT DISULFID 399..466
FT /evidence="ECO:0000269|PubMed:18468997,
FT ECO:0000269|PubMed:19097997"
FT DISULFID 419..424
FT /evidence="ECO:0000269|PubMed:18468997,
FT ECO:0000269|PubMed:19097997"
FT MUTAGEN 62
FT /note="Q->A: Slightly reduces catalytic activity."
FT /evidence="ECO:0000269|PubMed:19097997"
FT MUTAGEN 107
FT /note="Y->F,Q: Slightly reduces catalytic activity."
FT /evidence="ECO:0000269|PubMed:19097997"
FT MUTAGEN 132
FT /note="D->N: Slightly reduces catalytic activity."
FT /evidence="ECO:0000269|PubMed:19097997"
FT MUTAGEN 175
FT /note="N->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:19097997"
FT MUTAGEN 176
FT /note="E->Q: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:19097997"
FT MUTAGEN 244
FT /note="Y->F,Q: Moderately reduces hydrolysis, and causes a
FT 10-fold reduction in transglycosylation activity."
FT /evidence="ECO:0000269|PubMed:19097997"
FT MUTAGEN 275
FT /note="E->Q: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:19097997"
FT MUTAGEN 307
FT /note="Y->Q: Moderately reduces catalytic activity."
FT /evidence="ECO:0000269|PubMed:19097997"
FT MUTAGEN 404
FT /note="F->A: Slightly reduces catalytic activity."
FT /evidence="ECO:0000269|PubMed:19097997"
FT MUTAGEN 474
FT /note="Y->A: No effect."
FT /evidence="ECO:0000269|PubMed:19097997"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:5O9Q"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:5O9Q"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:5O9Q"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:5OA2"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:5O9Q"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:2W61"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:5O9Q"
FT HELIX 86..99
FT /evidence="ECO:0007829|PDB:5O9Q"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:5O9Q"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:5O9Q"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:5O9Q"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:5FIH"
FT HELIX 149..162
FT /evidence="ECO:0007829|PDB:5O9Q"
FT STRAND 168..178
FT /evidence="ECO:0007829|PDB:5O9Q"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:5O9Q"
FT HELIX 187..203
FT /evidence="ECO:0007829|PDB:5O9Q"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:5O9Q"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:5O9Q"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:5O9Q"
FT HELIX 222..228
FT /evidence="ECO:0007829|PDB:5O9Q"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:5OA2"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:5O9Q"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:5O9Q"
FT HELIX 257..264
FT /evidence="ECO:0007829|PDB:5O9Q"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:5O9Q"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:5O9Q"
FT HELIX 288..292
FT /evidence="ECO:0007829|PDB:5O9Q"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:5O9Q"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:5O9Q"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:5O9Q"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:5O9Q"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:5O9Q"
FT HELIX 332..342
FT /evidence="ECO:0007829|PDB:5O9Q"
FT HELIX 350..354
FT /evidence="ECO:0007829|PDB:5O9Q"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:5O9Q"
FT HELIX 387..396
FT /evidence="ECO:0007829|PDB:5O9Q"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:5O9Q"
FT HELIX 410..421
FT /evidence="ECO:0007829|PDB:5O9Q"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:5O9Q"
FT TURN 431..434
FT /evidence="ECO:0007829|PDB:5O9Q"
FT TURN 438..441
FT /evidence="ECO:0007829|PDB:5O9Q"
FT HELIX 444..453
FT /evidence="ECO:0007829|PDB:5O9Q"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:5O9Q"
FT HELIX 477..480
FT /evidence="ECO:0007829|PDB:5O9Q"
FT HELIX 490..501
FT /evidence="ECO:0007829|PDB:2W61"
SQ SEQUENCE 555 AA; 62362 MW; 15395E4F137DAC7F CRC64;
MNKKQNFYAA IIVAIFLCLQ LSHGSSGVSF EKTPAIKIVG NKFFDSESGE QFFIKGIAYQ
LQRSEEELSN ANGAFETSYI DALADPKICL RDIPFLKMLG VNTLRVYAID PTKSHDICME
ALSAEGMYVL LDLSEPDISI NRENPSWDVH IFERYKSVID AMSSFPNLLG YFAGNEVTND
HTNTFASPFV KAAIRDAKEY ISHSNHRKIP VGYSTNDDAM TRDNLARYFV CGDVKADFYG
INMYEWCGYS TYGTSGYRER TKEFEGYPIP VFFSEFGCNL VRPRPFTEVS ALYGNKMSSV
WSGGLAYMYF EEENEYGVVK INDNDGVDIL PDFKNLKKEF AKADPKGITE EEYLTAKEPT
EVESVECPHI AVGVWEANEK LPETPDRSKC ACLDEILPCE IVPFGAESGK YEEYFSYLCS
KVDCSDILAN GKTGEYGEFS DCSVEQKLSL QLSKLYCKIG ANDRHCPLND KNVYFNLESL
QPLTSESICK NVFDSIRNIT YNHGDYSKSN PSRSKESLNV KYPSSEEREN DGTIAFKTSG
FVILLISMIA AGILL
