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P07683

- AMYG_RHIOR

UniProt

P07683 - AMYG_RHIOR

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Protein

Glucoamylase 1

Gene
N/A
Organism
Rhizopus oryzae (Mucormycosis agent) (Rhizopus arrhizus var. delemar)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei279 – 2791SubstrateBy similarity
Active sitei336 – 3361Proton acceptorPROSITE-ProRule annotation
Active sitei339 – 3391Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

  1. glucan 1,4-alpha-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Protein family/group databases

CAZyiCBM21. Carbohydrate-Binding Module Family 21.
GH15. Glycoside Hydrolase Family 15.
mycoCLAPiGLA15E_RHIOR.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucoamylase 1 (EC:3.2.1.3)
Short name:
Gluc 1
Alternative name(s):
1,4-alpha-D-glucan glucohydrolase
Glucan 1,4-alpha-glucosidase
Cleaved into the following 2 chains:
Glucoamylase 2
Short name:
Gluc 2
Glucoamylase 3
Short name:
Gluc 3
OrganismiRhizopus oryzae (Mucormycosis agent) (Rhizopus arrhizus var. delemar)
Taxonomic identifieri64495 [NCBI]
Taxonomic lineageiEukaryotaFungiFungi incertae sedisEarly diverging fungal lineagesMucoromycotinaMucoralesMucorineaeRhizopodaceaeRhizopus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Add
BLAST
Chaini26 – 604579Glucoamylase 1PRO_0000001472Add
BLAST
Chaini116 – 604489Glucoamylase 3PRO_0000001473Add
BLAST
Chaini159 – 604446Glucoamylase 2PRO_0000001474Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi122 – 1221N-linked (GlcNAc...)Sequence Analysis
Glycosylationi167 – 1671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi230 – 2301N-linked (GlcNAc...)Sequence Analysis
Glycosylationi236 – 2361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi564 – 5641N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Structurei

Secondary structure

1
604
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 4415
Beta strandi46 – 527
Beta strandi55 – 573
Beta strandi59 – 679
Beta strandi78 – 803
Beta strandi82 – 865
Beta strandi93 – 997
Beta strandi102 – 11514
Beta strandi117 – 1204
Beta strandi122 – 1254

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DJMNMR-A26-131[»]
ProteinModelPortaliP07683.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07683.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 130105CBM21PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni26 – 11590Adsorption to raw starchAdd
BLAST
Regioni116 – 604489Starch degradationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 15 family.Curated
Contains 1 CBM21 (carbohydrate binding type-21) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di1.50.10.10. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR005036. CBM_21.
IPR000165. Glucoamylase.
IPR011613. Glyco_hydro_15.
[Graphical view]
PfamiPF03370. CBM_21. 1 hit.
PF00723. Glyco_hydro_15. 1 hit.
[Graphical view]
PRINTSiPR00736. GLHYDRLASE15.
SUPFAMiSSF48208. SSF48208. 1 hit.
PROSITEiPS51159. CBM21. 1 hit.
PS00820. GLUCOAMYLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07683-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQLFNLPLKV SFFLVLSYFS LLVSAASIPS SASVQLDSYN YDGSTFSGKI
60 70 80 90 100
YVKNIAYSKK VTVIYADGSD NWNNNGNTIA ASYSAPISGS NYEYWTFSAS
110 120 130 140 150
INGIKEFYIK YEVSGKTYYD NNNSANYQVS TSKPTTTTAT ATTTTAPSTS
160 170 180 190 200
TTTPPSRSEP ATFPTGNSTI SSWIKKQEGI SRFAMLRNIN PPGSATGFIA
210 220 230 240 250
ASLSTAGPDY YYAWTRDAAL TSNVIVYEYN TTLSGNKTIL NVLKDYVTFS
260 270 280 290 300
VKTQSTSTVC NCLGEPKFNP DASGYTGAWG RPQNDGPAER ATTFILFADS
310 320 330 340 350
YLTQTKDASY VTGTLKPAIF KDLDYVVNVW SNGCFDLWEE VNGVHFYTLM
360 370 380 390 400
VMRKGLLLGA DFAKRNGDST RASTYSSTAS TIANKISSFW VSSNNWIQVS
410 420 430 440 450
QSVTGGVSKK GLDVSTLLAA NLGSVDDGFF TPGSEKILAT AVAVEDSFAS
460 470 480 490 500
LYPINKNLPS YLGNSIGRYP EDTYNGNGNS QGNSWFLAVT GYAELYYRAI
510 520 530 540 550
KEWIGNGGVT VSSISLPFFK KFDSSATSGK KYTVGTSDFN NLAQNIALAA
560 570 580 590 600
DRFLSTVQLH AHNNGSLAEE FDRTTGLSTG ARDLTWSHAS LITASYAKAG

APAA
Length:604
Mass (Da):65,162
Last modified:November 1, 1995 - v2
Checksum:i78421F1AAA93ADB9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D00049 Genomic DNA. Translation: BAA00033.1.
PIRiJP0001.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D00049 Genomic DNA. Translation: BAA00033.1 .
PIRi JP0001.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DJM NMR - A 26-131 [» ]
ProteinModelPortali P07683.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P07683.
ChEMBLi CHEMBL4449.

Protein family/group databases

CAZyi CBM21. Carbohydrate-Binding Module Family 21.
GH15. Glycoside Hydrolase Family 15.
mycoCLAPi GLA15E_RHIOR.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P07683.

Family and domain databases

Gene3Di 1.50.10.10. 1 hit.
InterProi IPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR005036. CBM_21.
IPR000165. Glucoamylase.
IPR011613. Glyco_hydro_15.
[Graphical view ]
Pfami PF03370. CBM_21. 1 hit.
PF00723. Glyco_hydro_15. 1 hit.
[Graphical view ]
PRINTSi PR00736. GLHYDRLASE15.
SUPFAMi SSF48208. SSF48208. 1 hit.
PROSITEi PS51159. CBM21. 1 hit.
PS00820. GLUCOAMYLASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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] [Europe PMC]
    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] [Europe PMC]
    Cited for: HOMOLOGY, PREDICTED SECONDARY STRUCTURE.

Entry informationi

Entry nameiAMYG_RHIOR
AccessioniPrimary (citable) accession number: P07683
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 1, 1995
Last modified: October 1, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3