AMYG_ASPKA
ID AMYG_ASPKA Reviewed; 639 AA.
AC P23176;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Glucoamylase I;
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=gaI;
OS Aspergillus kawachii (White koji mold) (Aspergillus awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1069201;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX DOI=10.1271/bbb1961.53.923;
RA Hayashida S., Kuroda K., Ohta K., Kuhara S., Fukuda K., Sakaki Y.;
RT "Molecular cloning of the glucoamylase I gene of Aspergillus awamori var.
RT kawachi for localization of the raw-starch-affinity site.";
RL Agric. Biol. Chem. 53:923-929(1989).
RN [2]
RP PROTEIN SEQUENCE OF 494-538.
RX DOI=10.1271/bbb1961.53.135;
RA Hayashida S., Nakahara K., Kuroda K., Miyata T., Iwanaga S.;
RT "Structure of the raw-starch-affinity site on the Aspergillus awamori var.
RT kawachi glucoamylase I molecule.";
RL Agric. Biol. Chem. 53:135-141(1989).
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; D00427; BAA00331.1; -; Genomic_DNA.
DR PIR; JT0479; JT0479.
DR AlphaFoldDB; P23176; -.
DR BMRB; P23176; -.
DR SMR; P23176; -.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR CAZy; GH15; Glycoside Hydrolase Family 15.
DR GlyConnect; 173; 4 O-Linked glycans.
DR VEuPathDB; FungiDB:AKAW_08979; -.
DR GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd05811; CBM20_glucoamylase; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR034836; CBM20_glucoamylase.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR011613; GH15-like.
DR InterPro; IPR000165; Glucoamylase.
DR InterPro; IPR008291; Glucoamylase_SBD.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF00686; CBM_20; 1.
DR Pfam; PF00723; Glyco_hydro_15; 1.
DR PIRSF; PIRSF001031; Glu-a-glcsd_SBD; 1.
DR PRINTS; PR00736; GLHYDRLASE15.
DR SMART; SM01065; CBM_2; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF49452; SSF49452; 1.
DR PROSITE; PS51166; CBM20; 1.
DR PROSITE; PS00820; GLUCOAMYLASE; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Signal.
FT SIGNAL 1..18
FT PROPEP 19..24
FT /id="PRO_0000001463"
FT CHAIN 25..639
FT /note="Glucoamylase I"
FT /id="PRO_0000001464"
FT DOMAIN 532..639
FT /note="CBM20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT REGION 494..531
FT /note="Raw-starch-adsorbable GP-I sequence"
FT REGION 497..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 199
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT ACT_SITE 202
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 464
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 466
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 467
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 475
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 476
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 482
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 483
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 485
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 487
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 491
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 495
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 498
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 499
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 500
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 501
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 503
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 505
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 507
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 511
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 512
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 513
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 514
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 516
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 517
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 519
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 521
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 523
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 524
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 525
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 526
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 527
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 528
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 529
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 530
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 531
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 533
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 534
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000250"
FT DISULFID 233..236
FT /evidence="ECO:0000250"
FT DISULFID 245..472
FT /evidence="ECO:0000250"
FT DISULFID 285..293
FT /evidence="ECO:0000250"
SQ SEQUENCE 639 AA; 68272 MW; E112B31A4DD8DD6B CRC64;
MSFRSLLALS GLVCSGLANV ISKRATLDSW LSNEATVART AILNNIGADG AWVSGADSGI
VVASPSTDNP DYFYTWTRDS GLVIKTLVDL FRNGDTDLLS TIEHYISSQA IIQGVSNPSG
DLSSGGLGEP KFNVDETAYT GSWGRPQRDG PALRATAMIG FGQVLLDNGY TSAATEIVWP
LVRNDLSYVA QYWNQTGYDL WEEVNGSSFF TIAVQHRALV EGSAFATAVG SSCSWCDSQA
PQILCYLQSF WTGSYILANF DSRRSGKDTN TLLGSIHTFD PEAGCDDSTF QPCSPRALAN
HKEVVDSFRS IYTLNDGLSD SEAVAVGRYP EDSYYNGNPW FQSTLAAAEQ LYDALYQWDK
QGSLEITDVS LDFFKALYSG AATGTYSSSS STYSSIVSAV KTFADGFVSI VETHAASNGS
LSEQFDKSDG DELSARDLTW SYAALLTANN RRNSVVPPSW GETSASSWPG TCAATSASGT
YSSVTVTSWP SIVATGGTTT TATTTGSGGV TSTSKTTTTA SKTSTTTSST SCTTPTAVAV
TFDLTATTTY GENIYLVGSI SQLGDWETSD GIALSADKYT SSNPLWYVTV TLPAGESFEY
KFIRVESDDS VEWESDPNRE YTVPQACGES TATVTDTWR
