ID   AMYD_RHIO9              Reviewed;         452 AA.
AC   I1BYW6;
DT   01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Glucoamylase amyD {ECO:0000303|PubMed:17503147};
DE            EC=3.2.1.3;
DE   AltName: Full=1,4-alpha-D-glucan glucohydrolase amyD {ECO:0000305};
DE   AltName: Full=Amyloglucosidase D {ECO:0000305};
DE   AltName: Full=Glucan 1,4-alpha-glucosidase amyD {ECO:0000305};
DE   Flags: Precursor;
GN   Name=amyD {ECO:0000303|PubMed:17503147}; ORFNames=RO3G_06101;
OS   Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS   43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=246409;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880;
RX   PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA   Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA   Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA   Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA   Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA   Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA   Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT   "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT   whole-genome duplication.";
RL   PLoS Genet. 5:E1000549-E1000549(2009).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX   PubMed=17503147; DOI=10.1007/s00284-006-0655-8;
RA   Mertens J.A., Skory C.D.;
RT   "Isolation and characterization of two genes that encode active
RT   glucoamylase without a starch binding domain from Rhizopus oryzae.";
RL   Curr. Microbiol. 54:462-466(2007).
CC   -!- FUNCTION: Consecutively hydrolyzes alpha(1-4) glycosidic bonds from the
CC       non-reducing ends of starch, resulting in the production of glucose. It
CC       also has a limited ability to produce glucose through the hydrolysis of
CC       amylopectin alpha(1-6) linkages. {ECO:0000269|PubMed:17503147}.
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:0000269|PubMed:17503147};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:17503147}.
CC   -!- INDUCTION: Expressed in presence of arabinose, cellobiose, fructose,
CC       glucose, glycerol, maltose, pullulan, soluble starch, or xylose.
CC       {ECO:0000269|PubMed:17503147}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family. {ECO:0000305}.
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DR   EMBL; CH476735; EIE81396.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1BYW6; -.
DR   SMR; I1BYW6; -.
DR   STRING; 936053.I1BYW6; -.
DR   CLAE; GLA15D_RHIOR; -.
DR   EnsemblFungi; EIE81396; EIE81396; RO3G_06101.
DR   VEuPathDB; FungiDB:RO3G_06101; -.
DR   eggNOG; ENOG502QPM2; Eukaryota.
DR   InParanoid; I1BYW6; -.
DR   OMA; DLTWSYG; -.
DR   OrthoDB; 589046at2759; -.
DR   Proteomes; UP000009138; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR011613; GH15-like.
DR   InterPro; IPR000165; Glucoamylase.
DR   Pfam; PF00723; Glyco_hydro_15; 1.
DR   PRINTS; PR00736; GLHYDRLASE15.
DR   SUPFAM; SSF48208; SSF48208; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..452
FT                   /note="Glucoamylase amyD"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000432728"
FT   ACT_SITE        189
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT   ACT_SITE        192
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P69327"
FT   CARBOHYD        23
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        217
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        411
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   452 AA;  51550 MW;  4DA277CAB9387FCD CRC64;
     MFIGYLLLIL AIFGFYYSIQ QINGSSIFKK KNLLDDWISK QNTISFNSIL KNINPSGTPR
     GFVAASLSTS YPDYFYTWTR DAALVVRVLS DLPETDDDVL KDYIDFQIHI QNTPTVCHCL
     GEPKFNPDGT GYTGSWGRPQ NDGPAERAIT FIKIANRLKN SAYVSQKIVP ALEKDLDYIL
     QVWEQPCFDL WEEVDGVHFY TLMAMQRALL DAFDFFNLSK YRSTAYRIQE KIERFWSSEE
     NYIRVTHEVR EGANKPSGLD VSVLMAANMF ATTREGFFTP GSDKVLATAA AIEKSFSSIY
     PINKNLQPDL GVAIGRYPED VYDGYGSSKG NPWFLTTAAY VELYYLAMKE WKQTGLQINA
     VNKPFFERFL PIDDHCIYYS PDSQQLKEII NLVSLEADKF LATIQYHQQR NGSMSEQYSR
     YDGYMQGARD LTWSHAAFIS AIKAREGNSV AF