ID   GLAB_BACFR              Reviewed;         595 AA.
AC   Q64XV2;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Alpha-1,3-galactosidase B;
DE            EC=3.2.1.n1 {ECO:0000250|UniProtKB:Q5LGZ8};
DE            EC=3.2.1.n2 {ECO:0000250|UniProtKB:Q5LGZ8};
DE   AltName: Full=Exo-alpha-galactosidase B;
DE            EC=3.2.1.22 {ECO:0000250|UniProtKB:Q5LGZ8};
DE   Flags: Precursor;
GN   Name=glaB; OrderedLocusNames=BF0923;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT   regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
CC   -!- FUNCTION: Alpha-galactosidase. Removes both branched alpha-1,3-linked
CC       galactose residues of blood group B antigens and linear alpha-1,3-
CC       linked galactose structures. {ECO:0000250|UniProtKB:Q5LGZ8}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing branched (1->3)-alpha-D-
CC         galactosidic residues, producing free D-galactose.; EC=3.2.1.n1;
CC         Evidence={ECO:0000250|UniProtKB:Q5LGZ8};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing linear (1->3)-alpha-D-
CC         galactosidic residues, producing free D-galactose.; EC=3.2.1.n2;
CC         Evidence={ECO:0000250|UniProtKB:Q5LGZ8};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose
CC         residues in alpha-D-galactosides, including galactose
CC         oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22;
CC         Evidence={ECO:0000250|UniProtKB:Q5LGZ8};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 110 family. B subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AP006841; BAD47674.1; -; Genomic_DNA.
DR   RefSeq; WP_011202199.1; NC_006347.1.
DR   RefSeq; YP_098208.1; NC_006347.1.
DR   AlphaFoldDB; Q64XV2; -.
DR   SMR; Q64XV2; -.
DR   STRING; 295405.BF0923; -.
DR   CAZy; GH110; Glycoside Hydrolase Family 110.
DR   EnsemblBacteria; BAD47674; BAD47674; BF0923.
DR   KEGG; bfr:BF0923; -.
DR   PATRIC; fig|295405.11.peg.926; -.
DR   HOGENOM; CLU_017693_0_0_10; -.
DR   OMA; ATHFSGC; -.
DR   Proteomes; UP000002197; Chromosome.
DR   GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.160.20.10; -; 2.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; Repeat; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..595
FT                   /note="Alpha-1,3-galactosidase B"
FT                   /id="PRO_0000348477"
FT   REPEAT          432..454
FT                   /note="PbH1 1"
FT   REPEAT          455..477
FT                   /note="PbH1 2"
FT   REPEAT          488..541
FT                   /note="PbH1 3"
SQ   SEQUENCE   595 AA;  66982 MW;  9B80163520E631B7 CRC64;
     MKTILLFALS LLLSLSVSDV CAQERVYDIS QFGLKANSKK NASPVVRKAI AKIKAECRDG
     EKVILRFPAG RYNFHEAGST VREYYISNHD QDNPKKVGIA LEDMKNLTID GQGSEFVFYG
     RMIPVSLLRS ENCVLKNFSI DFEQPHIAQV QVVENDPEKG ITFEPAPWVD YRISKDSVFE
     GLGEGWVMRY SWGIAFDGKT KHVVYNTSDI GCPTKGAFEV APRRICSPKW KDARLVPGTV
     VAMRGWGRPT PGIFMSHDVN TSLLDVKVHY AEGMGLLAQL CEDITLDGFG VCLKGNNDPR
     YFTTQADATH FSGCKGKIVS KNGLYEGMMD DAINVHGTYL KVIKRVDDHT LIGRYMHDQS
     WGFEWGRPGD DVQFVRSETM ELIGKQNQIT AIRPYDKGEI QGAREFSITF KEAIDPAINE
     KSGFGIENLT WTPEVLFAGN TIRNNRARGT LFSTPKKTVV EDNLFDHTSG TAILLCGDCN
     GWFETGACRD VTIRRNRFIN ALTNMFQFTN AVISIYPEIP NLKDQQKYFH GGKDGGIVIE
     DNEFDTFDAP ILYAKSVDGL IFRNNVIKTN TEFKPFHWNK DRFLLERVTN VKISE