ID   AMYG_CLOS0              Reviewed;         702 AA.
AC   P29761;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Glucoamylase;
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=cga;
OS   Clostridium sp. (strain G0005).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=72582;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=1633799; DOI=10.1111/j.1432-1033.1992.tb17064.x;
RA   Ohnishi H., Kitamura H., Minowa T., Sakai H., Ohta T.;
RT   "Molecular cloning of a glucoamylase gene from a thermophilic Clostridium
RT   and kinetics of the cloned enzyme.";
RL   Eur. J. Biochem. 207:413-418(1992).
CC   -!- FUNCTION: CGA has typical kinetic properties for a glucoamylase, but
CC       this bacterial enzyme had higher isomaltose-hydrolyzing activity than
CC       other eukaryotic glucoamylases.
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   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor.
CC   -!- MISCELLANEOUS: High activity towards 1,6-glycosidic bonds.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family. {ECO:0000305}.
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DR   EMBL; D12818; BAA02251.1; -; Genomic_DNA.
DR   AlphaFoldDB; P29761; -.
DR   SMR; P29761; -.
DR   CAZy; GH15; Glycoside Hydrolase Family 15.
DR   SABIO-RK; P29761; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0016757; F:glycosyltransferase activity; IEA:UniProt.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd07430; GH15_N; 1.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.70.98.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR011613; GH15-like.
DR   InterPro; IPR000165; Glucoamylase.
DR   InterPro; IPR006425; Glucoamylase_bac.
DR   InterPro; IPR015220; Glucodextranase_N.
DR   Pfam; PF09137; Glucodextran_N; 1.
DR   Pfam; PF00723; Glyco_hydro_15; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
DR   TIGRFAMs; TIGR01535; glucan_glucosid; 1.
DR   PROSITE; PS00820; GLUCOAMYLASE; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cell membrane; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Lipoprotein; Membrane; Palmitate;
KW   Polysaccharide degradation; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           22..702
FT                   /note="Glucoamylase"
FT                   /id="PRO_0000001481"
FT   ACT_SITE        452
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT   ACT_SITE        455
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT   BINDING         342
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   LIPID           22
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000305"
FT   LIPID           22
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   702 AA;  78658 MW;  955EB4D0AD569546 CRC64;
     MSRKLIKYLP LLVLASSVLS GCSNNVSSIK IDRFNNISAV NGPGEEDTWA SAQKQGVGTA
     NNYVSKVWFT LANGAISEVY YPTIDTADVK EIKFIVTDGK SFVSDETKDT ISKVEKFTDK
     SLGYKLVNTD KKGRYRITKE IFTDVKRNSL IMKAKFEALE GSIHDYKLYL AYDPHIKNQG
     SYNEGYVIKA NNNEMLMAKR DNVYTALSSN IGWKGYSIGY YKVNDIMTDL DENKQMTKHY
     DSARGNIIEG AEIDLKKNSQ FEIVLSFGNS EDEAVKASIE TLSENYDSLK SAYIDEWEKY
     CNSLNNFNGK ANSLYYNSMM ILKASEDKTN KGAYIASLSI PWGDGQGDDN TGGYHLVWSR
     DLYHVANAFI AAGDVDSANR SLDYLAKVVK DNGMIPQNTW ISGKPYWTGI QLDEQADPII
     LSYRLRRYDL YDSLVKPLAD FIIKMGPKTG QERWEEIGGY SPATMAAEVA GLTCAAYIAE
     QNKDYESAQK YQEKADNWQK LIDNLTYTEH GPLENGQYYI RIAGLPDPNA DFTISIANGG
     GVYDQKEIVD PSFLELVRLG VKSPDDPKIL NTLRVVDSTI KVDTPKGPSW YRYNHDGYGE
     PSKTELYHGA GKGRLWPLLT GERGMYEIAA GKDATPYLKA MENFANEGGI ISEQVWEDTG
     LPTDSASPLN WAHAEYVVLF PSNIEHKVLD MPDIVYKRYV AK