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B1V8K7

- GLAA_STRGU

UniProt

B1V8K7 - GLAA_STRGU

Protein

Alpha-1,3-galactosidase A

Gene

glaA

Organism
Streptomyces griseoplanus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 27 (01 Oct 2014)
      Sequence version 1 (20 May 2008)
      Previous versions | rss
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    Functioni

    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 activityi

    Hydrolysis of terminal, non-reducing branched (1->3)-alpha-D-galactosidic residues, producing free D-galactose.
    Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.

    GO - Molecular functioni

    1. raffinose alpha-galactosidase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiGH110. Glycoside Hydrolase Family 110.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-1,3-galactosidase A (EC:3.2.1.n1)
    Alternative name(s):
    Exo-alpha-galactosidase A (EC:3.2.1.22)
    SgGal110A
    Gene namesi
    Name:glaA
    Synonyms:gla
    OrganismiStreptomyces griseoplanus
    Taxonomic identifieri66896 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

    Pathology & Biotechi

    Biotechnological usei

    Specifically cleaves the branched blood group B antigen at neutral pH with low consumption of recombinant enzyme. It is therefore a good candidate to participate in the development of universal red blood cells by removing blood group B antigen.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 727727Alpha-1,3-galactosidase APRO_0000348460Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliB1V8K7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati336 – 35823PbH1 1Add
    BLAST
    Repeati461 – 48323PbH1 2Add
    BLAST
    Repeati484 – 50623PbH1 3Add
    BLAST
    Repeati517 – 53822PbH1 4Add
    BLAST
    Repeati551 – 57222PbH1 5Add
    BLAST
    Repeati574 – 60330PbH1 6Add
    BLAST

    Sequence similaritiesi

    Contains 6 PbH1 repeats.Curated

    Keywords - Domaini

    Repeat

    Family and domain databases

    Gene3Di2.160.20.10. 4 hits.
    InterProiIPR003343. Big_2.
    IPR008964. Invasin/intimin_cell_adhesion.
    IPR006626. PbH1.
    IPR012334. Pectin_lyas_fold.
    IPR011050. Pectin_lyase_fold/virulence.
    [Graphical view]
    PfamiPF02368. Big_2. 1 hit.
    [Graphical view]
    SMARTiSM00710. PbH1. 6 hits.
    [Graphical view]
    SUPFAMiSSF49373. SSF49373. 1 hit.
    SSF51126. SSF51126. 3 hits.

    Sequencei

    Sequence statusi: Complete.

    B1V8K7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGTATAQPAL RPQTSTVIGG LHGAAVLDNT GRTVIDVTDF GADPSGKADS    50
    AAAVSAAMAH AKTVGGPTTL HFPTGTYHIW PERTPKRELY VSNTVGSDQA 100
    FRTKNIGILV EDMRDVVVDG GGSRIVNHGF QTVFAAIRSS DVRFTNFSQT 150
    WVAPKTVDIT VADAGVVSGQ AYRIIDIPET YDYAVEGTSV RWNGERGPAT 200
    GQPYWTGTNS FDYSQVHDPA TNRTWRTSNP VFPERHEDHR PRRRQVRITY 250
    GDSTAPGDRG YVYQMREVTR DTPGALFWES SRVTVDHLRL GYLHGFGIVG 300
    QLSEDIGIDS VTFKADRGSG RVTSGFADHI QMSGVKGTVR ITNSVFDNPQ 350
    DDPINIHGTY LQATAAERET LQLRYMHNET SGFPQFYPGD TIELVDKRTM 400
    LAAPGATAKV VSVTGPTGSG VPAGTDPDTY LRTMTVVLDR TLPAAVLAAP 450
    GDYVAENTTY TPTVEITGNT FQAVPTRGIL VTTRRPVRIE NNRFDGMSMA 500
    SIYISSDARS WYESGPVRNV TIRGNVFDRP ASPVIFFDPT NQDFVAGQPV 550
    HRNVLIEDND FNLTGGTILS GRGVGGLTFR DNRVERYPHL RLTGPSRALR 600
    VGDTTTVTTD APPPSHTSPL FTFDGADDIT LANNTYGNGF NKRVNTANMD 650
    VSEITVTADG LALNADSISS APVAVSYSSS RPKVATVDSE GVVKALSGGT 700
    TSITARATIG GVRVTSNPVK VVVATER 727
    Length:727
    Mass (Da):78,244
    Last modified:May 20, 2008 - v1
    Checksum:i059E250ED79FB764
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti66 – 661G → I AA sequence (PubMed:17401360)Curated
    Sequence conflicti76 – 761T → G AA sequence (PubMed:17401360)Curated
    Sequence conflicti492 – 4921N → S AA sequence (PubMed:17401360)Curated
    Sequence conflicti496 – 4961G → D AA sequence (PubMed:17401360)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM259273 Genomic DNA. Translation: CAJ90659.1.

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    The juice of life - Issue 98 of October 2008

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM259273 Genomic DNA. Translation: CAJ90659.1 .

    3D structure databases

    ProteinModelPortali B1V8K7.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH110. Glycoside Hydrolase Family 110.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.160.20.10. 4 hits.
    InterProi IPR003343. Big_2.
    IPR008964. Invasin/intimin_cell_adhesion.
    IPR006626. PbH1.
    IPR012334. Pectin_lyas_fold.
    IPR011050. Pectin_lyase_fold/virulence.
    [Graphical view ]
    Pfami PF02368. Big_2. 1 hit.
    [Graphical view ]
    SMARTi SM00710. PbH1. 6 hits.
    [Graphical view ]
    SUPFAMi SSF49373. SSF49373. 1 hit.
    SSF51126. SSF51126. 3 hits.
    ProtoNeti Search...

    Publicationsi

    1. "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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ENZYME ACTIVITY.
    2. Cited for: PROTEIN SEQUENCE OF 34-77; 144-153; 273-280 AND 489-497, CATALYTIC ACTIVITY.

    Entry informationi

    Entry nameiGLAA_STRGU
    AccessioniPrimary (citable) accession number: B1V8K7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 2, 2008
    Last sequence update: May 20, 2008
    Last modified: October 1, 2014
    This is version 27 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3