EXG1_YEAST
ID EXG1_YEAST Reviewed; 448 AA.
AC P23776; D6VYU4; Q9UR92;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Glucan 1,3-beta-glucosidase I/II;
DE EC=3.2.1.58;
DE AltName: Full=Exo-1,3-beta-glucanase I/II;
DE AltName: Full=Soluble cell wall protein 6;
DE Flags: Precursor;
GN Name=EXG1; Synonyms=BGL1, SCW6; OrderedLocusNames=YLR300W;
GN ORFNames=L8003.3;
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 [GENOMIC DNA], AND PROTEIN SEQUENCE OF 41-48.
RX PubMed=1900250; DOI=10.1016/0378-1119(91)90049-h;
RA Vazquez de Aldana C.R., Correa J., San Segundo P., Bueno A., Nebreda A.R.,
RA Mendez E., del Rey F.;
RT "Nucleotide sequence of the exo-1,3-beta-glucanase-encoding gene, EXG1, of
RT the yeast Saccharomyces cerevisiae.";
RL Gene 97:173-182(1991).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP PROTEIN SEQUENCE OF 41-86.
RX PubMed=2125957; DOI=10.1111/j.1574-6968.1990.tb03796.x;
RA Ramirez M., Munoz M.D., Basco R.D., Gimenez-Gallego G., Hernandez L.M.,
RA Larriba G.;
RT "Two glycosylation patterns for a single protein (exoglucanase) in
RT Saccharomyces cerevisiae.";
RL FEMS Microbiol. Lett. 59:43-48(1990).
RN [6]
RP PROTEIN SEQUENCE OF 41-65.
RX PubMed=8488724; DOI=10.1002/yea.320090303;
RA Basco R.D., Munoz M.D., Hernandez L.M., Vazquez de Aldana C., Larriba G.;
RT "Reduced efficiency in the glycosylation of the first sequon of
RT Saccharomyces cerevisiae exoglucanase leads to the synthesis and secretion
RT of a new glycoform of the molecule.";
RL Yeast 9:221-234(1993).
RN [7]
RP PROTEIN SEQUENCE OF 41-51, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 96099 / S288c / SEY6210;
RX PubMed=9748433; DOI=10.1128/jb.180.19.5030-5037.1998;
RA Cappellaro C., Mrsa V., Tanner W.;
RT "New potential cell wall glucanases of Saccharomyces cerevisiae and their
RT involvement in mating.";
RL J. Bacteriol. 180:5030-5037(1998).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 41-448, AND GLYCOSYLATION AT
RP ASN-165 AND ASN-325.
RX PubMed=14730348; DOI=10.1038/nsmb715;
RA Taylor S.C., Ferguson A.D., Bergeron J.J.M., Thomas D.Y.;
RT "The ER protein folding sensor UDP-glucose glycoprotein-glucosyltransferase
RT modifies substrates distant to local changes in glycoprotein
RT conformation.";
RL Nat. Struct. Mol. Biol. 11:128-134(2004).
CC -!- FUNCTION: Glucanases possibly play a role in cell expansion during
CC growth, in cell-cell fusion during mating, and in spore release during
CC sporulation. This enzyme hydrolyzes both 1,3-beta- and 1,6-beta-
CC linkages and even has beta-glucosidase activity. It could also function
CC biosynthetically as a transglycosylase.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Successive hydrolysis of beta-D-glucose units from the non-
CC reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.;
CC EC=3.2.1.58;
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:9748433}.
CC Secreted {ECO:0000269|PubMed:9748433}.
CC -!- MISCELLANEOUS: Present with 4280 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; M34341; AAA34599.1; -; Genomic_DNA.
DR EMBL; U17243; AAB67345.1; -; Genomic_DNA.
DR EMBL; AY693069; AAT93088.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09610.1; -; Genomic_DNA.
DR PIR; JN0118; JN0118.
DR RefSeq; NP_013403.1; NM_001182188.1.
DR PDB; 1H4P; X-ray; 1.75 A; A/B=41-448.
DR PDBsum; 1H4P; -.
DR AlphaFoldDB; P23776; -.
DR SMR; P23776; -.
DR BioGRID; 31564; 111.
DR DIP; DIP-6384N; -.
DR IntAct; P23776; 3.
DR STRING; 4932.YLR300W; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR CLAE; EXG5A_YEAST; -.
DR iPTMnet; P23776; -.
DR COMPLUYEAST-2DPAGE; P23776; -.
DR MaxQB; P23776; -.
DR PaxDb; P23776; -.
DR PRIDE; P23776; -.
DR EnsemblFungi; YLR300W_mRNA; YLR300W; YLR300W.
DR GeneID; 851007; -.
DR KEGG; sce:YLR300W; -.
DR SGD; S000004291; EXG1.
DR VEuPathDB; FungiDB:YLR300W; -.
DR eggNOG; ENOG502QPYU; Eukaryota.
DR GeneTree; ENSGT00940000176313; -.
DR HOGENOM; CLU_004624_0_1_1; -.
DR InParanoid; P23776; -.
DR OMA; YWTWKAE; -.
DR BioCyc; YEAST:YLR300W-MON; -.
DR EvolutionaryTrace; P23776; -.
DR PRO; PR:P23776; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P23776; protein.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IDA:SGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR GO; GO:0004338; F:glucan exo-1,3-beta-glucosidase activity; ISS:SGD.
DR GO; GO:0006073; P:cellular glucan metabolic process; IMP:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; ISS:SGD.
DR GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Cell wall biogenesis/degradation;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..40
FT /evidence="ECO:0000269|PubMed:1900250,
FT ECO:0000269|PubMed:2125957, ECO:0000269|PubMed:8488724,
FT ECO:0000269|PubMed:9748433"
FT /id="PRO_0000007892"
FT CHAIN 41..448
FT /note="Glucan 1,3-beta-glucosidase I/II"
FT /id="PRO_0000007893"
FT ACT_SITE 232
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 334
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14730348"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14730348"
FT CONFLICT 41
FT /note="Y -> Q (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="H -> G (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="R -> H (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1H4P"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1H4P"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:1H4P"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:1H4P"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:1H4P"
FT HELIX 99..113
FT /evidence="ECO:0007829|PDB:1H4P"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:1H4P"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:1H4P"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:1H4P"
FT HELIX 152..165
FT /evidence="ECO:0007829|PDB:1H4P"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:1H4P"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:1H4P"
FT HELIX 198..214
FT /evidence="ECO:0007829|PDB:1H4P"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:1H4P"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:1H4P"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:1H4P"
FT HELIX 240..246
FT /evidence="ECO:0007829|PDB:1H4P"
FT HELIX 248..257
FT /evidence="ECO:0007829|PDB:1H4P"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:1H4P"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:1H4P"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:1H4P"
FT STRAND 289..296
FT /evidence="ECO:0007829|PDB:1H4P"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:1H4P"
FT HELIX 309..323
FT /evidence="ECO:0007829|PDB:1H4P"
FT STRAND 327..335
FT /evidence="ECO:0007829|PDB:1H4P"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:1H4P"
FT TURN 344..347
FT /evidence="ECO:0007829|PDB:1H4P"
FT TURN 373..376
FT /evidence="ECO:0007829|PDB:1H4P"
FT HELIX 378..380
FT /evidence="ECO:0007829|PDB:1H4P"
FT HELIX 383..400
FT /evidence="ECO:0007829|PDB:1H4P"
FT TURN 401..404
FT /evidence="ECO:0007829|PDB:1H4P"
FT STRAND 405..409
FT /evidence="ECO:0007829|PDB:1H4P"
FT HELIX 421..426
FT /evidence="ECO:0007829|PDB:1H4P"
FT HELIX 442..444
FT /evidence="ECO:0007829|PDB:1H4P"
SQ SEQUENCE 448 AA; 51311 MW; F0AD512E410375BD CRC64;
MLSLKTLLCT LLTVSSVLAT PVPARDPSSI QFVHEENKKR YYDYDHGSLG EPIRGVNIGG
WLLLEPYITP SLFEAFRTND DNDEGIPVDE YHFCQYLGKD LAKSRLQSHW STFYQEQDFA
NIASQGFNLV RIPIGYWAFQ TLDDDPYVSG LQESYLDQAI GWARNNSLKV WVDLHGAAGS
QNGFDNSGLR DSYKFLEDSN LAVTTNVLNY ILKKYSAEEY LDTVIGIELI NEPLGPVLDM
DKMKNDYLAP AYEYLRNNIK SDQVIIIHDA FQPYNYWDDF MTENDGYWGV TIDHHHYQVF
ASDQLERSID EHIKVACEWG TGVLNESHWT VCGEFAAALT DCTKWLNSVG FGARYDGSWV
NGDQTSSYIG SCANNDDIAY WSDERKENTR RYVEAQLDAF EMRGGWIIWC YKTESSLEWD
AQRLMFNGLF PQPLTDRKYP NQCGTISN
