ID V5FE43_BYSSN Unreviewed; 622 AA.
AC V5FE43;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Glucoamylase {ECO:0000256|PIRNR:PIRNR001031};
DE EC=3.2.1.3 {ECO:0000256|PIRNR:PIRNR001031};
DE AltName: Full=1,4-alpha-D-glucan glucohydrolase {ECO:0000256|PIRNR:PIRNR001031};
DE AltName: Full=Glucan 1,4-alpha-glucosidase {ECO:0000256|PIRNR:PIRNR001031};
GN ORFNames=PVAR5_4285 {ECO:0000313|EMBL:GAD95639.1};
OS Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD95639.1, ECO:0000313|Proteomes:UP000018001};
RN [1] {ECO:0000313|Proteomes:UP000018001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA Oka T., Ekino K., Fukuda K., Nomura Y.;
RT "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL Genome Announc. 2:E0116213-E0116213(2014).
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:0000256|ARBA:ARBA00001863,
CC ECO:0000256|PIRNR:PIRNR001031};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family.
CC {ECO:0000256|ARBA:ARBA00006188, ECO:0000256|PIRNR:PIRNR001031}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAD95639.1}.
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DR EMBL; BAUL01000135; GAD95639.1; -; Genomic_DNA.
DR AlphaFoldDB; V5FE43; -.
DR SMR; V5FE43; -.
DR eggNOG; ENOG502QPM2; Eukaryota.
DR HOGENOM; CLU_012173_1_0_1; -.
DR InParanoid; V5FE43; -.
DR OrthoDB; 1586242at2759; -.
DR Proteomes; UP000018001; Unassembled WGS sequence.
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; Immunoglobulins; 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; IPR046966; Glucoamylase_active_site.
DR InterPro; IPR008291; Glucoamylase_SBD.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR31616:SF12; GLUCOAMYLASE-RELATED; 1.
DR PANTHER; PTHR31616; TREHALASE; 1.
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; Six-hairpin glycosidases; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51166; CBM20; 1.
DR PROSITE; PS00820; GLUCOAMYLASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|PIRNR:PIRNR001031};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR001031};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001031};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|PIRNR:PIRNR001031};
KW Reference proteome {ECO:0000313|Proteomes:UP000018001};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..622
FT /note="Glucoamylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004732895"
FT DOMAIN 515..622
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT ACT_SITE 214
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001031-1"
FT ACT_SITE 217
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001031-1"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001031-2"
SQ SEQUENCE 622 AA; 65797 MW; 090811BD2CD24EAB CRC64;
MGQITAMLKY FAQILSAVSI IQGTTGVVSG GAPVAPRATG SLDSWLATES PYALQGVLAN
IGPDGTDASG ASSGIVIASP SKSDPDYFYT WTRDAALTLK CLVDTFIAGN SDLQSTIQNY
ISAQAYLQTV SNPSGGLSTG GLGEPKFNVD ETAFTGAWGR PQRDGPALRA TAMIAYAKWL
IANGETSLAD SIIWPIVQND LSYVTQYWNS TGFDLWEEVS GSSFFTTAVQ HRALVEGNSL
AEQLNHTCSN CVSQAPQVLC FLQSYWTGSY VLANFGSSRS GKDANSLLGS IHTFDPDGGC
DDSTFQPCSA RALANHKVVT DSFRSVYSIN SGIAQGQAVA VGRYPEDSYQ GGNPWYLCTL
SAAELLYDAL YQWDRAGELT ITDVSLAFFQ DIYSDAAVGT YQSSSTTYSD ITDAVRTYAD
GYMSIAQKYA PSSGALAEQF SRSDGTPLSA GDLTWSYAAL LTAVARRNAT VPASWGEPSA
SSVPSACSAT SAAGPYSTAT NTNWGGSSTT TGSCTTTPTA VAVTFDVLAT TSYGENVYVV
GSVSALGSWD TDSAVALSAN KYTSSNPLWY GTVTLPAGES VEYKYIKKET DGSIVWESDP
NRDYQVPQKC GTTTAEVDDT WR
//
