AMYG_NEUCR
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 03-AUG-2022, entry version 164.
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; 5141.EFNCRP00000001634; -.
DR Allergome; 10750; Neu cr Glucoamylase.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR CAZy; GH15; Glycoside Hydrolase Family 15.
DR EnsemblFungi; EAA27730; EAA27730; NCU01517.
DR GeneID; 3873129; -.
DR KEGG; ncr:NCU01517; -.
DR HOGENOM; CLU_012173_1_0_1; -.
DR InParanoid; P14804; -.
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; -; 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; 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
