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Protein
Submitted name:

Glucoamylase

Gene

amyA

Organism
Rhizopus oryzae (Mucormycosis agent) (Rhizopus arrhizus var. delemar)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi26 – 261ZincCombined sources
Metal bindingi37 – 371ZincCombined sources
Binding sitei83 – 831GlucoseCombined sources
Binding sitei93 – 931GlucoseCombined sources

GO - Molecular functioni

  1. glucan 1,4-alpha-glucosidase activity Source: InterPro
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. polysaccharide metabolic process Source: InterPro
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Submitted name:
GlucoamylaseImported
Gene namesi
Name:amyAImported
OrganismiRhizopus oryzae (Mucormycosis agent) (Rhizopus arrhizus var. delemar)Imported
Taxonomic identifieri64495 [NCBI]
Taxonomic lineageiEukaryotaFungiFungi incertae sedisEarly diverging fungal lineagesMucoromycotinaMucoralesMucorineaeRhizopodaceaeRhizopus

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V8MX-ray2.30A/B/C/D26-131[»]
4EIBX-ray1.86A/B26-131[»]
ProteinModelPortaliB7XC04.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni54 – 596Glucose bindingCombined sources

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.

B7XC04-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQLFNLPLKV SFFLVLSYFS LLVSAASIPS SASVQLDSYN YDGSTFSGKI
60 70 80 90 100
YVKNIAYSKK VTVVYADGSD NWNNNGNIIA ASFSGPISGS NYEYWTFSAS
110 120 130 140 150
VKGIKEFYIK YEVSGKTYYD NNNSANYQVS TSKPTTTTTA TTTTTAPSTS
160 170 180 190 200
TTTRPSSSEP ATFPTGNSTI SSWIKKQEDI SRFAMLRNIN PPGSATGFIA
210 220 230 240 250
ASLSTAGPDY YYAWTRDAAL TSNVIVYEYN TTLSGNKTIL NVLKDYVTFS
260 270 280 290 300
VKTQSTSTVC NCLGEPKFNP DGSGYTGAWG RPQNDGPAER ATTFVLFADS
310 320 330 340 350
YLTQTKDASY VTGTLKPAIF KDLDYVVNVW SNGCFDLWEE VNGVHFYTLM
360 370 380 390 400
VMRKGLLLGA DFAKRNGDST RASTYSSTAS TIANKISSFW VSSNNWVQVS
410 420 430 440 450
QSVTGGVSKK GLDVSTLLAA NLGSVDDGFF TPGSEKILAT AVAVEDSFAS
460 470 480 490 500
LYPINKNLPS YLGNAIGRYP EDTYNGNGNS QGNPWFLAVT GYAELYYRAI
510 520 530 540 550
KEWISNGGVT VSSISLPFFK KFDSSATSGK KYTVGTSDFN NLAQNIALAA
560 570 580 590 600
DRFLSTVQLH APKNGSLAEE FDRTTGFSTG ARDLTWSHAS LITASYAKAG

APAA
Length:604
Mass (Da):65,198
Last modified:March 3, 2009 - v1
Checksum:i2B426455F3D4200D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB444727 Genomic DNA. Translation: BAH09876.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB444727 Genomic DNA. Translation: BAH09876.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V8MX-ray2.30A/B/C/D26-131[»]
4EIBX-ray1.86A/B26-131[»]
ProteinModelPortaliB7XC04.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]
ProtoNetiSearch...

Publicationsi

  1. "Crystal structures of the starch-binding domain from Rhizopus oryzae glucoamylase reveal a polysaccharide-binding path."
    Tung J.Y., Chang M.D., Chou W.I., Liu Y.Y., Yeh Y.H., Chang F.Y., Lin S.C., Qiu Z.L., Sun Y.J.
    Biochem. J. 416:27-36(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 26-131 IN COMPLEX WITH GLUCOSE AND ZINC.
  2. "Comparison of sucrose-hydrolyzing enzymes produced by Rhizopus oryzae and Amylomyces rouxii."
    Watanabe T., Oda Y.
    Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: NBRC 4785Imported.
  3. "Crystal structure of circular permuted RoCBM21 (CP90): dimerisation and proximity of binding sites."
    Stephen P., Cheng K.C., Lyu P.C.
    PLoS ONE 7:e50488-e50488(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 26-131.

Entry informationi

Entry nameiB7XC04_RHIOR
AccessioniPrimary (citable) accession number: B7XC04
Entry historyi
Integrated into UniProtKB/TrEMBL: March 3, 2009
Last sequence update: March 3, 2009
Last modified: February 4, 2015
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.