ID   AMYG_NEUCR              Reviewed;         626 AA.
AC   P14804; Q7RV62; Q9P5U5;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   30-APR-2003, sequence version 3.
DT   27-MAR-2024, entry version 169.
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=gla-1; ORFNames=B5O22.70, NCU01517;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=8221928; DOI=10.1007/bf00351793;
RA   Stone P.J., Makoff A.J., Parish J.H., Radford A.;
RT   "Cloning and sequence analysis of the glucoamylase gene of Neurospora
RT   crassa.";
RL   Curr. Genet. 24:205-211(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
RN   [4]
RP   PROTEIN SEQUENCE OF 36-65.
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RA   Koh-Luar S.I., Parish J.H., Bleasby A.J., Pappin D.J.C., Ainley K.,
RA   Johansen F.E., Radford A.;
RT   "Exported proteins of Neurospora crassa: 1-glucoamylase.";
RL   Enzyme Microb. Technol. 11:692-695(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA27730.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; X67291; CAA47707.1; -; Genomic_DNA.
DR   EMBL; AL355932; CAB91426.1; -; Genomic_DNA.
DR   EMBL; CM002237; EAA27730.2; ALT_INIT; Genomic_DNA.
DR   PIR; S36364; S36364.
DR   RefSeq; XP_956966.2; XM_951873.3.
DR   AlphaFoldDB; P14804; -.
DR   SMR; P14804; -.
DR   STRING; 367110.P14804; -.
DR   Allergome; 10750; Neu cr Glucoamylase.
DR   CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR   CAZy; GH15; Glycoside Hydrolase Family 15.
DR   GlyCosmos; P14804; 3 sites, No reported glycans.
DR   PaxDb; 5141-EFNCRP00000001634; -.
DR   EnsemblFungi; EAA27730; EAA27730; NCU01517.
DR   GeneID; 3873129; -.
DR   KEGG; ncr:NCU01517; -.
DR   HOGENOM; CLU_012173_1_0_1; -.
DR   InParanoid; P14804; -.
DR   OrthoDB; 1586242at2759; -.
DR   Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR   GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR   GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..35
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000001469"
FT   CHAIN           36..626
FT                   /note="Glucoamylase"
FT                   /id="PRO_0000001470"
FT   DOMAIN          520..626
FT                   /note="CBM20"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT   ACT_SITE        211
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT   ACT_SITE        214
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        206
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        217
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        82
FT                   /note="Missing (in Ref. 1; CAA47707)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        550
FT                   /note="A -> R (in Ref. 1; CAA47707)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        560
FT                   /note="V -> L (in Ref. 1; CAA47707)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   626 AA;  66475 MW;  54E5BDDBA7A3E349 CRC64;
     MHLVSSLLVV GAAFQAVLGL PDPLHEKRHS DIIKRSVDSY IQTETPIAQK NLLCNIGASG
     CRASGAASGV VVASPSKSSP DYWYTWTRDA ALVTKLIVDE FTNDYNTTLQ NTIQAYAAAQ
     AKLQGVSNPS GSLSNGAGLG EPKFMVDLQQ FTGAWGRPQR DGPPLRAIAL IGYGKWLVSN
     GYADTAKSII WPIVKNDLAY TAQYWNNTGF DLWEEVNSSS FFTIAASHRA LVEGSAFAKS
     VGSSCSACDA IAPQILCFQQ SFWSNSGYII SNFVNYRSGK DINSVLTSIH NFDPAAGCDV
     NTFQPCSDRA LANHKVVVDS MRFWGVNSGR TAGKAAAVGR YAEDVYYNGN PWYLATLAAA
     EQLYDAVYVW KKQGSITVTS TSLAFFKDLV PSVSTGTYSS SSSTYTAIIN AVTTYADGFV
     DIVAQYTPSD GSLAEQFDKD SGAPLSATHL TWSYASFLSA AARRAGIVPP SWGAASANSL
     PGSCSASTVA GSYATATATS FPANLTPAST TVTPPTQTGC AADHEVLVTF NEKVTTSYGQ
     TVKVVGSIAA LGNWAPASGV TLSAKQYSSS NPLWSTTIAL PQGTSFKYKY VVVNSDGSVK
     WENDPDRSYA VGTDCASTAT LDDTWR
//