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Q9F234 (AGL2_BACTQ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Alpha-glucosidase 2
EC=3.2.1.20
Alternative name(s):
Alpha-glucosidase II
OrganismBacillus thermoamyloliquefaciens
Taxonomic identifier1425 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length787 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.

Subunit structure

Homohexamer.

Sequence similarities

Belongs to the glycosyl hydrolase 31 family.

Ontologies

Keywords
   Molecular functionGlycosidase
Hydrolase
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

maltose alpha-glucosidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 787787Alpha-glucosidase 2
PRO_0000185368

Sites

Active site4071 By similarity
Active site4101 By similarity
Active site4841Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9F234 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 6BDD837E2C3304BF

FASTA78791,072
        10         20         30         40         50         60 
MLEDTSFAIQ PEQDDKTQET HRIDIGNMHT FSHTEHVFSF HCDTGIVKIR FYREDIVRIA 

        70         80         90        100        110        120 
FNPFGETSLS TSVAVVKEPE KVDASVHETE EEVTLTSAKQ TVVLQKRPFR VRIYDNHGRL 

       130        140        150        160        170        180 
LVAEGKKGMA FTYQGEVCCF KMMDEADHFY GFGEKTGFLD KRGETMTMWN TDVYAPHNPE 

       190        200        210        220        230        240 
TDPLYQSHPY FMTVRNGSAH GIFFDNTYKT TFDFQTATDE YCFSAEGGAI DYYVFAGPTP 

       250        260        270        280        290        300 
KDVLEQYTDL TGRMPLPPKW ALGYHQSRYS YETEQEVREI AQTFIEKDIP LDVIYLDIHY 

       310        320        330        340        350        360 
MNGYRVFTFD RNRFPNLKQL IADLKQKGIR VVPIVDPGVK EDPEYVIYQE GIRHDYFCKY 

       370        380        390        400        410        420 
IEGNVYFGEV WPGKSAFPDF TNKKVRKWWG EKHQFYTDLG IEGIWNDMNE PSVFNETKTM 

       430        440        450        460        470        480 
DVKVIHDNDG DPKTHRELHN VYGFMMGEAT YKGMKKLLNG KRPFLLTRAG FSGIQRYAAV 

       490        500        510        520        530        540 
WTGDNRSFWE HLQMSLPMCM NLGLSGVAFC GPDVGGFAHN TNGELLTRWM QVGAFTPYFR 

       550        560        570        580        590        600 
NHCAIGFRRQ EPWAFGEKYE RIIKKYIRLR YQWLPHLYTL FAEAHETGAP VMRPLFFEYP 

       610        620        630        640        650        660 
DDENTYNLYD EFLVGANVLI APIMTPSTTR RVAYFPKGNW VDYWTGEVLE GGQYHLISAD 

       670        680        690        700        710        720 
LETLPIFIKQ GSAIALGDVK RSTEMPDEHR TVHIYKANGG KATYVLYDDD GQTFSYEKGD 

       730        740        750        760        770        780 
YLRMYIEVEY GENSVHIVTK SEGTYQPSWK LSFAIHHATE QTKVTIDGNE QNAIFDPHQR 


ILLIQSE

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References

[1]"The primary structure of the subunit in Bacillus thermoamyloliquefaciens KP1071 molecular weight 540,000 homohexameric alpha-glucosidase II belonging to the glycosyl hydrolase family 31."
Kashiwabara S., Azuma S., Tsuduki M., Suzuki Y.
Biosci. Biotechnol. Biochem. 64:1379-1393(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: KP1071.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB012238 Genomic DNA. Translation: BAA76396.1.

3D structure databases

ProteinModelPortalQ9F234.
ModBaseSearch...

Protein family/group databases

CAZyGH31. Glycoside Hydrolase Family 31.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.2.1.20. 7482.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR025887. Glyco_hydro_31_N_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR22762. PTHR22762. 1 hit.
PfamPF13802. Gal_mutarotas_2. 1 hit.
PF01055. Glyco_hydro_31. 1 hit.
[Graphical view]
SUPFAMSSF74650. Gal_mut_like. 1 hit.
SSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAGL2_BACTQ
AccessionPrimary (citable) accession number: Q9F234
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: March 1, 2001
Last modified: April 3, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

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