ID   B7XC04_RHIOR            Unreviewed;       604 AA.
AC   B7XC04;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 70.
DE   RecName: Full=glucan 1,4-alpha-glucosidase {ECO:0000256|ARBA:ARBA00012593};
DE            EC=3.2.1.3 {ECO:0000256|ARBA:ARBA00012593};
DE   AltName: Full=1,4-alpha-D-glucan glucohydrolase {ECO:0000256|ARBA:ARBA00033473};
DE   AltName: Full=Glucan 1,4-alpha-glucosidase {ECO:0000256|ARBA:ARBA00033442};
GN   Name=amyA {ECO:0000313|EMBL:BAH09876.1};
OS   Rhizopus oryzae (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=64495 {ECO:0000313|EMBL:BAH09876.1};
RN   [1] {ECO:0007829|PDB:2V8L, ECO:0007829|PDB:2V8M}
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 26-131 IN COMPLEX WITH GLUCOSE
RP   AND ZINC.
RX   PubMed=18588504; DOI=10.1042/BJ20080580;
RA   Tung J.Y., Chang M.D., Chou W.I., Liu Y.Y., Yeh Y.H., Chang F.Y., Lin S.C.,
RA   Qiu Z.L., Sun Y.J.;
RT   "Crystal structures of the starch-binding domain from Rhizopus oryzae
RT   glucoamylase reveal a polysaccharide-binding path.";
RL   Biochem. J. 416:27-36(2008).
RN   [2] {ECO:0000313|EMBL:BAH09876.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NBRC 4785 {ECO:0000313|EMBL:BAH09876.1};
RA   Watanabe T., Oda Y.;
RT   "Comparison of sucrose-hydrolyzing enzymes produced by Rhizopus oryzae and
RT   Amylomyces rouxii.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0007829|PDB:4EIB}
RP   X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 26-131.
RX   PubMed=23226294; DOI=10.1371/journal.pone.0050488;
RA   Stephen P., Cheng K.C., Lyu P.C.;
RT   "Crystal structure of circular permuted RoCBM21 (CP90): dimerisation and
RT   proximity of binding sites.";
RL   PLoS ONE 7:e50488-e50488(2012).
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         Evidence={ECO:0000256|ARBA:ARBA00001863};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family.
CC       {ECO:0000256|ARBA:ARBA00006188}.
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DR   EMBL; AB444727; BAH09876.1; -; Genomic_DNA.
DR   PDB; 2V8L; X-ray; 1.80 A; A=26-131.
DR   PDB; 2V8M; X-ray; 2.30 A; A/B/C/D=26-131.
DR   PDB; 4EIB; X-ray; 1.86 A; A/B=19-114.
DR   PDBsum; 2V8L; -.
DR   PDBsum; 2V8M; -.
DR   PDBsum; 4EIB; -.
DR   AlphaFoldDB; B7XC04; -.
DR   SMR; B7XC04; -.
DR   CAZy; CBM21; Carbohydrate-Binding Module Family 21.
DR   CAZy; GH15; Glycoside Hydrolase Family 15.
DR   GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005976; P:polysaccharide metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.60.40.2440; Carbohydrate binding type-21 domain; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR005036; CBM21_dom.
DR   InterPro; IPR038175; CBM21_dom_sf.
DR   InterPro; IPR011613; GH15-like.
DR   InterPro; IPR000165; Glucoamylase.
DR   InterPro; IPR046966; Glucoamylase_active_site.
DR   PANTHER; PTHR31616:SF11; GLUCOAMYLASE, INTRACELLULAR SPORULATION-SPECIFIC; 1.
DR   PANTHER; PTHR31616; TREHALASE; 1.
DR   Pfam; PF03370; CBM_21; 1.
DR   Pfam; PF00723; Glyco_hydro_15; 1.
DR   PRINTS; PR00736; GLHYDRLASE15.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS51159; CBM21; 1.
DR   PROSITE; PS00820; GLUCOAMYLASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:2V8L, ECO:0007829|PDB:2V8M};
KW   Metal-binding {ECO:0007829|PDB:2V8L}; Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0007829|PDB:2V8L}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..604
FT                   /note="glucan 1,4-alpha-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002865665"
FT   DOMAIN          26..130
FT                   /note="CBM21"
FT                   /evidence="ECO:0000259|PROSITE:PS51159"
FT   REGION          129..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         26
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0007829|PDB:2V8L"
FT   BINDING         37
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0007829|PDB:2V8L"
SQ   SEQUENCE   604 AA;  65198 MW;  2B426455F3D4200D CRC64;
     MQLFNLPLKV SFFLVLSYFS LLVSAASIPS SASVQLDSYN YDGSTFSGKI YVKNIAYSKK
     VTVVYADGSD NWNNNGNIIA ASFSGPISGS NYEYWTFSAS VKGIKEFYIK YEVSGKTYYD
     NNNSANYQVS TSKPTTTTTA TTTTTAPSTS TTTRPSSSEP ATFPTGNSTI SSWIKKQEDI
     SRFAMLRNIN PPGSATGFIA ASLSTAGPDY YYAWTRDAAL TSNVIVYEYN TTLSGNKTIL
     NVLKDYVTFS VKTQSTSTVC NCLGEPKFNP DGSGYTGAWG RPQNDGPAER ATTFVLFADS
     YLTQTKDASY VTGTLKPAIF KDLDYVVNVW SNGCFDLWEE VNGVHFYTLM VMRKGLLLGA
     DFAKRNGDST RASTYSSTAS TIANKISSFW VSSNNWVQVS QSVTGGVSKK GLDVSTLLAA
     NLGSVDDGFF TPGSEKILAT AVAVEDSFAS LYPINKNLPS YLGNAIGRYP EDTYNGNGNS
     QGNPWFLAVT GYAELYYRAI KEWISNGGVT VSSISLPFFK KFDSSATSGK KYTVGTSDFN
     NLAQNIALAA DRFLSTVQLH APKNGSLAEE FDRTTGFSTG ARDLTWSHAS LITASYAKAG
     APAA
//