AMYG_SCHOC
ID AMYG_SCHOC Reviewed; 958 AA.
AC P22861; Q92336;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Glucoamylase 1;
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=GAM1;
OS Schwanniomyces occidentalis (Yeast) (Debaryomyces occidentalis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Schwanniomyces.
OX NCBI_TaxID=27300;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 26076 / DSM 3794 / CBS 2864 / BCRC 22059 / NCYC 954 / NRRL
RC Y-2470;
RX PubMed=1979298; DOI=10.1016/0378-1119(90)90421-m;
RA Dohmen R.J., Strasser A.W.M., Dahlems U.M., Hollenberg C.P.;
RT "Cloning of the Schwanniomyces occidentalis glucoamylase gene (GAM1) and
RT its expression in Saccharomyces cerevisiae.";
RL Gene 95:111-121(1990).
RN [2]
RP SIMILARITY TO OTHER FAMILY 31 MEMBERS.
RX PubMed=1743281; DOI=10.1016/0014-5793(91)81353-a;
RA Naim H.Y., Niermann T., Kleinhans U., Hollenberg C.P., Strasser A.W.M.;
RT "Striking structural and functional similarities suggest that intestinal
RT sucrase-isomaltase, human lysosomal alpha-glucosidase and Schwanniomyces
RT occidentalis glucoamylase are derived from a common ancestral gene.";
RL FEBS Lett. 294:109-112(1991).
CC -!- FUNCTION: This glucoamylase has a specificity toward both alpha-1,4 and
CC alpha-1,6 linkages.
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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10066};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M60207; AAA33923.1; -; Genomic_DNA.
DR PIR; JN0102; JN0102.
DR AlphaFoldDB; P22861; -.
DR SMR; P22861; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR CLAE; GLA31A_DEBOC; -.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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; 2.60.40.1180; -; 2.
DR InterPro; IPR031727; Gal_mutarotase_N.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR030458; Glyco_hydro_31_AS.
DR InterPro; IPR030459; Glyco_hydro_31_CS.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF01055; Glyco_hydro_31; 1.
DR Pfam; PF16863; NtCtMGAM_N; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
DR PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..958
FT /note="Glucoamylase 1"
FT /id="PRO_0000018586"
FT ACT_SITE 470
FT /evidence="ECO:0000250"
FT ACT_SITE 473
FT /evidence="ECO:0000250"
FT ACT_SITE 638
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 602
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 813
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 907
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 958 AA; 106508 MW; 47938DB9BC308260 CRC64;
MIFLKLIKSI VIGLGLVSAI QAAPASSIGS SASASSSSES SQATIPNDVT LGVKQIPNIF
NDSAVDANAA AKGYDLVNVT NTPRGLTGIL KLKEATNIYG YDFDYLNLTV EYQADTRLNV
HIEPTDLSDV FVLPEHLVVK PLVEGDAQSY NFDNSDLVFE YSNTDFSFEV IRSSTKEVLF
STKGNPLVFS NQFIQFNSSL PKNHVITGLG ESIHGLVNEP GSVKTLFAND VGDPIDGNIY
GVHPVYLDQR YDTETTHAVY WRTSAIQEVL IGEESITWRA LSGVIDLYFF SGPTPKDAIQ
QYVKEIGLPA FQPYWSLGYH QCRWGYDTIE KLSEVVENFK KFNIPLETIW SDIDYMDSYK
DFTYDPHRFP LDEYRKFLDE LHKNNQHYVP ILDAAIYVPN PNNATDNEYQ PFHYGNETDV
FLKNPDGSLY IGAVWQVTLF SRFLSRKHSD MDKVIKDWYE LTPFDGIWAD MNEVSSFCVG
SCGTGKYFEN PAYPPFTVGS KATSYPVGFD VSNASEWKSI QSSISATAKT SSTSSVSSSS
STIDYMNTLA PGKGNINYPP YAIYNMQGDS DLATHAVSPN ATHADGTVEY DIHNLYGYLQ
ENATYHALLE VFPNKRPFMI SRSTFPRAGK WTGHWGGDNT ADWAYAYFSI PQAFSMGIAG
LPFFGADVCG FNGNSDSELC SRWMQLGSFF PFYRNHNYLG AIDQEPYVWE SVAEATRTSM
AIRYLLLPYY YTLLHESHTT GLPILRAFSW QFPNDRSLSG VDNQFFVGDG LVVTPVLEPG
VDKVKGVFPG AGKEEVYYDW YTQREVHFKD GKNETLDAPL GHIPLHIRGG NVLPTQEPGY
TVAESRQNPF GLIVALDNDG KAQGSLYLDD GESLVVDSSL LVSFSVSDNT LSASPSGDYK
ADQPLANVTI LGVGHKPKSV KFENANVDFT YKKSTVFVTG LDKYTKDGAF SKDFTITW
