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Reviewed, UniProtKB/Swiss-Prot P07683 (AMYG_RHIOR)

Last modified January 19, 2010. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Glucoamylase 1
      Short name=Gluc 1
    EC=3.2.1.3
Alternative name(s):
    Glucan 1,4-alpha-glucosidase
    1,4-alpha-D-glucan glucohydrolase
Cleaved into the following 2 chains:
    1- Recommended name:
            Glucoamylase 2
                Short name=Gluc 2
    2- Recommended name:
            Glucoamylase 3
                Short name=Gluc 3
OrganismRhizopus oryzae (Rhizopus delemar)
Taxonomic identifier64495 [NCBI]
Taxonomic lineageEukaryota › Fungi › Fungi incertae sedis › Basal fungal lineages › Mucoromycotina › Mucorales › Mucoraceae › Rhizopus

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Protein attributes

Sequence length604 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose.

Miscellaneous

Rhizopus glucoamylase exists in multiple forms, Gluc 1, Gluc 2, and Gluc 3, all of which hydrolyze gelatinized starch at similar rates, but only the largest one (Gluc 1) is able to adsorb raw starch.

Glucoamylase 3 may be 110-604 instead of 116-104.

Sequence similarities

Belongs to the glycosyl hydrolase 15 family.

Contains 1 CBM21 (carbohydrate binding type-21) domain.

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Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processpolysaccharide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionglucan 1,4-alpha-glucosidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525
Chain26 – 604579Glucoamylase 1
PRO_0000001472
Chain116 – 604489Glucoamylase 3
PRO_0000001473
Chain159 – 604446Glucoamylase 2
PRO_0000001474

Regions

Domain26 – 130105CBM21
Region26 – 11590Adsorption to raw starch
Region116 – 604489Starch degradation

Sites

Active site3361Proton acceptor By similarity
Active site3391Proton donor By similarity
Binding site2791Substrate By similarity

Amino acid modifications

Glycosylation1221N-linked (GlcNAc...) Potential
Glycosylation1671N-linked (GlcNAc...) Potential
Glycosylation2301N-linked (GlcNAc...) Potential
Glycosylation2361N-linked (GlcNAc...) Potential
Glycosylation5641N-linked (GlcNAc...) Potential

Secondary structure

1 ................... 604
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P07683-1 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 78421F1AAA93ADB9

FASTA60465,162
        10         20         30         40         50         60 
MQLFNLPLKV SFFLVLSYFS LLVSAASIPS SASVQLDSYN YDGSTFSGKI YVKNIAYSKK 

        70         80         90        100        110        120 
VTVIYADGSD NWNNNGNTIA ASYSAPISGS NYEYWTFSAS INGIKEFYIK YEVSGKTYYD 

       130        140        150        160        170        180 
NNNSANYQVS TSKPTTTTAT ATTTTAPSTS TTTPPSRSEP ATFPTGNSTI SSWIKKQEGI 

       190        200        210        220        230        240 
SRFAMLRNIN PPGSATGFIA ASLSTAGPDY YYAWTRDAAL TSNVIVYEYN TTLSGNKTIL 

       250        260        270        280        290        300 
NVLKDYVTFS VKTQSTSTVC NCLGEPKFNP DASGYTGAWG RPQNDGPAER ATTFILFADS 

       310        320        330        340        350        360 
YLTQTKDASY VTGTLKPAIF KDLDYVVNVW SNGCFDLWEE VNGVHFYTLM VMRKGLLLGA 

       370        380        390        400        410        420 
DFAKRNGDST RASTYSSTAS TIANKISSFW VSSNNWIQVS QSVTGGVSKK GLDVSTLLAA 

       430        440        450        460        470        480 
NLGSVDDGFF TPGSEKILAT AVAVEDSFAS LYPINKNLPS YLGNSIGRYP EDTYNGNGNS 

       490        500        510        520        530        540 
QGNSWFLAVT GYAELYYRAI KEWIGNGGVT VSSISLPFFK KFDSSATSGK KYTVGTSDFN 

       550        560        570        580        590        600 
NLAQNIALAA DRFLSTVQLH AHNNGSLAEE FDRTTGLSTG ARDLTWSHAS LITASYAKAG 


APAA

« Hide

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References

[1]"Rhizopus raw-starch-degrading glucoamylase: its cloning and expression in yeast."
Ashikari T., Nakamura N., Tanaka Y., Kiuchi N., Shibano Y., Tanaka T., Amachi T., Yoshizumi H.
Agric. Biol. Chem. 50:957-964(1986) [Agricola: IND86045328]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: SAM0034.
[2]"Comparison of amino acid sequences of three glucoamylases and their structure-function relationships."
Tanaka Y., Ashikari T., Nakamura N., Kiuchi N., Shibano Y., Amachi T., Yoshizumi H.
Agric. Biol. Chem. 50:965-969(1986) [Agricola: IND86045329]
Cited for: HOMOLOGY, PREDICTED SECONDARY STRUCTURE.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D00049 Genomic DNA. Translation: BAA00033.1.
PIRJP0001.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DJMNMR-A26-131[»]
2V8LX-ray1.80A26-131[»]
2V8MX-ray2.30A/B/C/D26-131[»]
ModBaseSearch...

Protein family/group databases

CAZyCBM21. Carbohydrate-Binding Module Family 21.
GH15. Glycoside Hydrolase Family 15.

Enzyme and pathway databases

BRENDA3.2.1.3. 141574.

Family and domain databases

InterProIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR005036. CBM_21.
IPR000165. Glyco_hydro_15.
IPR011613. Glyco_hydro_15_rel.
[Graphical view]
Gene3DG3DSA:1.50.10.10. CelA/Cel48F_cat. 1 hit.
PfamPF03370. CBM_21. 1 hit.
PF00723. Glyco_hydro_15. 1 hit.
[Graphical view]
PRINTSPR00736. GLHYDRLASE15.
PROSITEPS51159. CBM21. 1 hit.
PS00820. GLUCOAMYLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameAMYG_RHIOR
AccessionPrimary (citable) accession number: P07683
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 1, 1995
Last modified: January 19, 2010
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents