AMYG_SACFI
ID AMYG_SACFI Reviewed; 519 AA.
AC P08017;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Glucoamylase GLU1;
DE EC=3.2.1.3;
DE AltName: Full=1,4-alpha-D-glucan glucohydrolase;
DE AltName: Full=Glucan 1,4-alpha-glucosidase;
DE Flags: Precursor;
GN Name=GLU1;
OS Saccharomycopsis fibuligera (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycopsidaceae; Saccharomycopsis.
OX NCBI_TaxID=4944;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3114236; DOI=10.1128/jb.169.9.4171-4176.1987;
RA Itoh T., Ohtsuki I., Yamashita I., Fukui S.;
RT "Nucleotide sequence of the glucoamylase gene GLU1 in the yeast
RT Saccharomycopsis fibuligera.";
RL J. Bacteriol. 169:4171-4176(1987).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=9757101; DOI=10.1107/s0907444998002005;
RA Sevcik J., Solovicova A., Hostinova E., Gasperik J., Wilson K.S.,
RA Dauter Z.;
RT "Structure of glucoamylase from Saccharomycopsis fibuligera at 1.7-A
RT resolution.";
RL Acta Crystallogr. D 54:854-866(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues
CC successively from non-reducing ends of the chains with release of
CC beta-D-glucose.; EC=3.2.1.3;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family. {ECO:0000305}.
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DR EMBL; L25641; AAA83997.1; -; mRNA.
DR EMBL; M17355; AAA34649.1; -; Genomic_DNA.
DR PIR; A54549; A54549.
DR PDB; 1AYX; X-ray; 1.70 A; A=28-519.
DR PDB; 2F6D; X-ray; 1.60 A; A=28-519.
DR PDB; 2FBA; X-ray; 1.10 A; A=28-519.
DR PDBsum; 1AYX; -.
DR PDBsum; 2F6D; -.
DR PDBsum; 2FBA; -.
DR AlphaFoldDB; P08017; -.
DR SMR; P08017; -.
DR CAZy; GH15; Glycoside Hydrolase Family 15.
DR CLAE; GLA15A_SACFI; -.
DR BRENDA; 3.2.1.3; 2072.
DR EvolutionaryTrace; P08017; -.
DR GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR011613; GH15-like.
DR InterPro; IPR000165; Glucoamylase.
DR Pfam; PF00723; Glyco_hydro_15; 1.
DR PRINTS; PR00736; GLHYDRLASE15.
DR SUPFAM; SSF48208; SSF48208; 1.
DR PROSITE; PS00820; GLUCOAMYLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Signal.
FT SIGNAL 1..27
FT CHAIN 28..519
FT /note="Glucoamylase GLU1"
FT /id="PRO_0000001475"
FT ACT_SITE 234
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT ACT_SITE 237
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT HELIX 45..62
FT /evidence="ECO:0007829|PDB:2FBA"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:2FBA"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:2FBA"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:2FBA"
FT HELIX 95..111
FT /evidence="ECO:0007829|PDB:2FBA"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:2FBA"
FT HELIX 116..133
FT /evidence="ECO:0007829|PDB:2FBA"
FT HELIX 145..151
FT /evidence="ECO:0007829|PDB:2FBA"
FT HELIX 173..191
FT /evidence="ECO:0007829|PDB:2FBA"
FT HELIX 209..215
FT /evidence="ECO:0007829|PDB:2FBA"
FT HELIX 217..227
FT /evidence="ECO:0007829|PDB:2FBA"
FT HELIX 244..263
FT /evidence="ECO:0007829|PDB:2FBA"
FT HELIX 267..285
FT /evidence="ECO:0007829|PDB:2FBA"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:2FBA"
FT TURN 294..297
FT /evidence="ECO:0007829|PDB:2FBA"
FT HELIX 303..307
FT /evidence="ECO:0007829|PDB:2FBA"
FT HELIX 317..325
FT /evidence="ECO:0007829|PDB:2FBA"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:2F6D"
FT HELIX 341..357
FT /evidence="ECO:0007829|PDB:2FBA"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:2FBA"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:1AYX"
FT STRAND 380..385
FT /evidence="ECO:0007829|PDB:2FBA"
FT HELIX 390..410
FT /evidence="ECO:0007829|PDB:2FBA"
FT STRAND 414..417
FT /evidence="ECO:0007829|PDB:2FBA"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:2FBA"
FT HELIX 421..427
FT /evidence="ECO:0007829|PDB:2FBA"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:2FBA"
FT HELIX 438..440
FT /evidence="ECO:0007829|PDB:2FBA"
FT STRAND 441..446
FT /evidence="ECO:0007829|PDB:2FBA"
FT HELIX 451..474
FT /evidence="ECO:0007829|PDB:2FBA"
FT STRAND 483..485
FT /evidence="ECO:0007829|PDB:2FBA"
FT TURN 487..489
FT /evidence="ECO:0007829|PDB:2FBA"
FT STRAND 492..495
FT /evidence="ECO:0007829|PDB:2FBA"
FT HELIX 499..516
FT /evidence="ECO:0007829|PDB:2FBA"
SQ SEQUENCE 519 AA; 57539 MW; BE73035AD1B77652 CRC64;
MKFGVLFSVF AAIVSALPLQ EGPLNKRAYP SFEAYSNYKV DRTDLETFLD KQKEVSLYYL
LQNIAYPEGQ FNNGVPGTVI ASPSTSNPDY YYQWTRDSAI TFLTVLSELE DNNFNTTLAK
AVEYYINTSY NLQRTSNPSG SFDDENHKGL GEPKFNTDGS AYTGAWGRPQ NDGPALRAYA
ISRYLNDVNS LNEGKLVLTD SGDINFSSTE DIYKNIIKPD LEYVIGYWDS TGFDLWEENQ
GRHFFTSLVQ QKALAYAVDI AKSFDDGDFA NTLSSTASTL ESYLSGSDGG FVNTDVNHIV
ENPDLLQQNS RQGLDSATYI GPLLTHDIGE SSSTPFDVDN EYVLQSYYLL LEDNKDRYSV
NSAYSAGAAI GRYPEDVYNG DGSSEGNPWF LATAYAAQVP YKLAYDAKSA SNDITINKIN
YDFFNKYIVD LSTINSAYQS SDSVTIKSGS DEFNTVADNL VTFGDSFLQV ILDHINDDGS
LNEQLNRYTG YSTGAYSLTW SSGALLEAIR LRNKVKALA
