AMYG_RHIOR
ID AMYG_RHIOR Reviewed; 604 AA.
AC P07683;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Glucoamylase 1;
DE Short=Gluc 1;
DE EC=3.2.1.3;
DE AltName: Full=1,4-alpha-D-glucan glucohydrolase;
DE AltName: Full=Glucan 1,4-alpha-glucosidase;
DE Contains:
DE RecName: Full=Glucoamylase 2;
DE Short=Gluc 2;
DE Contains:
DE RecName: Full=Glucoamylase 3;
DE Short=Gluc 3;
DE Flags: Precursor;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SAM0034;
RX AGRICOLA=IND86045328;
RA Ashikari T., Nakamura N., Tanaka Y., Kiuchi N., Shibano Y., Tanaka T.,
RA Amachi T., Yoshizumi H.;
RT "Rhizopus raw-starch-degrading glucoamylase: its cloning and expression in
RT yeast.";
RL Agric. Biol. Chem. 50:957-964(1986).
RN [2]
RP HOMOLOGY, AND PREDICTED SECONDARY STRUCTURE.
RX AGRICOLA=IND86045329;
RA Tanaka Y., Ashikari T., Nakamura N., Kiuchi N., Shibano Y., Amachi T.,
RA Yoshizumi H.;
RT "Comparison of amino acid sequences of three glucoamylases and their
RT structure-function relationships.";
RL Agric. Biol. Chem. 50:965-969(1986).
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 -!- MISCELLANEOUS: Rhizopus glucoamylase exists in multiple forms, Gluc 1,
CC Gluc 2, and Gluc 3, all of which hydrolyze gelatinized starch at
CC similar rates, but only the largest one (Gluc 1) is able to adsorb raw
CC starch.
CC -!- MISCELLANEOUS: Glucoamylase 3 may be 110-604 instead of 116-604.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family. {ECO:0000305}.
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DR EMBL; D00049; BAA00033.1; -; Genomic_DNA.
DR PIR; JP0001; JP0001.
DR PDB; 2DJM; NMR; -; A=26-131.
DR PDBsum; 2DJM; -.
DR AlphaFoldDB; P07683; -.
DR SMR; P07683; -.
DR BindingDB; P07683; -.
DR ChEMBL; CHEMBL4449; -.
DR CAZy; CBM21; Carbohydrate-Binding Module Family 21.
DR CAZy; GH15; Glycoside Hydrolase Family 15.
DR CLAE; GLA15E_RHIOR; -.
DR BRENDA; 3.2.1.3; 5365.
DR EvolutionaryTrace; P07683; -.
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 Gene3D; 2.60.40.2440; -; 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 Pfam; PF03370; CBM_21; 1.
DR Pfam; PF00723; Glyco_hydro_15; 1.
DR PRINTS; PR00736; GLHYDRLASE15.
DR SUPFAM; SSF48208; SSF48208; 1.
DR PROSITE; PS51159; CBM21; 1.
DR PROSITE; PS00820; GLUCOAMYLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Signal.
FT SIGNAL 1..25
FT CHAIN 26..604
FT /note="Glucoamylase 1"
FT /id="PRO_0000001472"
FT CHAIN 116..604
FT /note="Glucoamylase 3"
FT /id="PRO_0000001473"
FT CHAIN 159..604
FT /note="Glucoamylase 2"
FT /id="PRO_0000001474"
FT DOMAIN 26..130
FT /note="CBM21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00491"
FT REGION 26..115
FT /note="Adsorption to raw starch"
FT REGION 116..604
FT /note="Starch degradation"
FT REGION 127..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 336
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT ACT_SITE 339
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 564
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT STRAND 30..44
FT /evidence="ECO:0007829|PDB:2DJM"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:2DJM"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:2DJM"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:2DJM"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:2DJM"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:2DJM"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:2DJM"
FT STRAND 102..115
FT /evidence="ECO:0007829|PDB:2DJM"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:2DJM"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:2DJM"
SQ SEQUENCE 604 AA; 65162 MW; 78421F1AAA93ADB9 CRC64;
MQLFNLPLKV SFFLVLSYFS LLVSAASIPS SASVQLDSYN YDGSTFSGKI YVKNIAYSKK
VTVIYADGSD NWNNNGNTIA ASYSAPISGS NYEYWTFSAS INGIKEFYIK YEVSGKTYYD
NNNSANYQVS TSKPTTTTAT ATTTTAPSTS TTTPPSRSEP ATFPTGNSTI SSWIKKQEGI
SRFAMLRNIN PPGSATGFIA ASLSTAGPDY YYAWTRDAAL TSNVIVYEYN TTLSGNKTIL
NVLKDYVTFS VKTQSTSTVC NCLGEPKFNP DASGYTGAWG RPQNDGPAER ATTFILFADS
YLTQTKDASY VTGTLKPAIF KDLDYVVNVW SNGCFDLWEE VNGVHFYTLM VMRKGLLLGA
DFAKRNGDST RASTYSSTAS TIANKISSFW VSSNNWIQVS QSVTGGVSKK GLDVSTLLAA
NLGSVDDGFF TPGSEKILAT AVAVEDSFAS LYPINKNLPS YLGNSIGRYP EDTYNGNGNS
QGNSWFLAVT GYAELYYRAI KEWIGNGGVT VSSISLPFFK KFDSSATSGK KYTVGTSDFN
NLAQNIALAA DRFLSTVQLH AHNNGSLAEE FDRTTGLSTG ARDLTWSHAS LITASYAKAG
APAA
