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Q826C5 (GLAA_STRAW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-1,3-galactosidase A

EC=3.2.1.n1
Alternative name(s):
Exo-alpha-galactosidase A
EC=3.2.1.22
SaGal110A
Gene names
Name:glaA
Ordered Locus Names:SAV_7268
OrganismStreptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680) [Complete proteome] [HAMAP]
Taxonomic identifier227882 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length625 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Alpha-galactosidase that specifically removes branched alpha-1,3-linked galactose residues present in blood group B antigens. Has no activity toward linear alpha-1,3-linked galactose residues.

Catalytic activity

Hydrolysis of terminal, non-reducing branched (1->3)-alpha-D-galactosidic residues, producing free D-galactose. Ref.4

Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids. Ref.4

Sequence similarities

Belongs to the glycosyl hydrolase 110 family. A subfamily.

Contains 5 PbH1 repeats.

Ontologies

Keywords
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Molecular_functionraffinose alpha-galactosidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Potential
Chain33 – 625593Alpha-1,3-galactosidase A
PRO_0000348474

Regions

Repeat342 – 36423PbH1 1
Repeat460 – 48223PbH1 2
Repeat483 – 50523PbH1 3
Repeat516 – 53722PbH1 4
Repeat573 – 61139PbH1 5

Sequences

Sequence LengthMass (Da)Tools
Q826C5 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 4B80A1A6C94D372E

FASTA62567,184
        10         20         30         40         50         60 
MAHGCSGGAM SRFVFLGVAL ALLGGATSPA AAAPRVTPVV VDVDDYGADP TGRTDSTPAV 

        70         80         90        100        110        120 
AAALRHAKSV DRPVRIVFSK GTYQLYPERA ETRELYMSNT VGADQRYRDK KIGLLVEDMH 

       130        140        150        160        170        180 
DVTVDGGGAK LVHHGLQTAF ASIRSTDVTF QNFSFDYAAP EVIDATVATT GVTDGHAYRV 

       190        200        210        220        230        240 
LKIPAGSPYR VNGTHITWLG ETSPATGQPY WSGVDGLQYT QIHDPEAQRT WRGDNPLFND 

       250        260        270        280        290        300 
VAAVTDLGGR RIRIDYTTAA RPADAGLVYQ MRLIERTEPG AFIWESKNVT MRSMNAYYLQ 

       310        320        330        340        350        360 
SFGVVGQFSE NISIDKVNFA PDPRSGRSTA SFADFVQMSG VKGKVSITRS LFDGPHDDPI 

       370        380        390        400        410        420 
NIHGTYLEVV GKPGPSTLTL AYKHPQTAGF PQFAPGDEVE FATKRTMTPL ADAHAQVTAV 

       430        440        450        460        470        480 
DGPSGMDHTK PLTTMTVTFD RPVPAGVETG GTVVENITAT PSVVISGNVF RNVPTRGILV 

       490        500        510        520        530        540 
TTRKPVLITG NRFDGMSMAS IYVSADAYQW YESGPVADLT IRGNSFTRPS GPVIFVEPTN 

       550        560        570        580        590        600 
QVIDPATPVH HNISVEHNSF DIGDVTVVNA KSVGGFAFTG NTVRRLDGAD HPPYTSPLFV 

       610        620 
FHGSSGIRIA RNHYDKGLNT SVVTD 

« Hide

References

« Hide 'large scale' references
[1]"Bacterial glycosidases for the production of universal red blood cells."
Liu Q.P., Sulzenbacher G., Yuan H., Bennett E.P., Pietz G., Saunders K., Spence J., Nudelman E., Levery S.B., White T., Neveu J.M., Lane W.S., Bourne Y., Olsson M.L., Henrissat B., Clausen H.
Nat. Biotechnol. 25:454-464(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.
[2]"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.
[3]"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
Nat. Biotechnol. 21:526-531(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.
[4]"Identification of a GH110 subfamily of alpha1,3-galactosidases: novel enzymes for removal of the alpha3Gal xenotransplantation antigen."
Liu Q.P., Yuan H., Bennett E.P., Levery S.B., Nudelman E., Spence J., Pietz G., Saunders K., White T., Olsson M.L., Henrissat B., Sulzenbacher G., Clausen H.
J. Biol. Chem. 283:8545-8554(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME ACTIVITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM109953 Genomic DNA. Translation: CAJ33349.1.
BA000030 Genomic DNA. Translation: BAC74979.1.
RefSeqNP_828444.1. NC_003155.4.

3D structure databases

ProteinModelPortalQ826C5.
ModBaseSearch...

Protein-protein interaction databases

STRING227882.SAV_7268.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC74979; BAC74979; SAV_7268.
GeneID1217418.
KEGGsma:SAV_7268.
PATRIC23728724. VBIStrAve112782_7700.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG77539.
HOGENOMHOG000049734.
OMALKLRFMH.
ProtClustDBCLSK823424.

Enzyme and pathway databases

BioCycSAVE227882:GJU1-7365-MONOMER.

Family and domain databases

Gene3D2.160.20.10. 3 hits.
InterProIPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
SMARTSM00710. PbH1. 5 hits.
[Graphical view]
SUPFAMSSF51126. Pectin_lyas_like. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGLAA_STRAW
AccessionPrimary (citable) accession number: Q826C5
Secondary accession number(s): A4Q8G4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: June 1, 2003
Last modified: May 1, 2013
This is version 58 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