ID   GLAB2_PHOV8             Reviewed;         605 AA.
AC   A6L2M8;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
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 B2;
DE            EC=3.2.1.22 {ECO:0000250|UniProtKB:Q5LGZ8};
DE   Flags: Precursor;
GN   Name=glaB2; OrderedLocusNames=BVU_2283;
OS   Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 /
OS   NBRC 14291 / NCTC 11154) (Bacteroides vulgatus).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Phocaeicola.
OX   NCBI_TaxID=435590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / NCTC
RC   11154;
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000139; ABR39942.1; -; Genomic_DNA.
DR   RefSeq; WP_011965552.1; NC_009614.1.
DR   AlphaFoldDB; A6L2M8; -.
DR   SMR; A6L2M8; -.
DR   STRING; 435590.BVU_2283; -.
DR   CAZy; GH110; Glycoside Hydrolase Family 110.
DR   EnsemblBacteria; ABR39942; ABR39942; BVU_2283.
DR   KEGG; bvu:BVU_2283; -.
DR   eggNOG; COG5434; Bacteria.
DR   HOGENOM; CLU_017693_0_0_10; -.
DR   OMA; RTENITI; -.
DR   OrthoDB; 1217730at2; -.
DR   BioCyc; BVUL435590:G1G59-2374-MON; -.
DR   Proteomes; UP000002861; 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; -; 1.
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; Reference proteome; Repeat; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..605
FT                   /note="Alpha-1,3-galactosidase B"
FT                   /id="PRO_0000348480"
FT   REPEAT          428..450
FT                   /note="PbH1 1"
FT   REPEAT          451..473
FT                   /note="PbH1 2"
FT   REPEAT          484..538
FT                   /note="PbH1 3"
SQ   SEQUENCE   605 AA;  68957 MW;  E7385BBB5AB7ADFF CRC64;
     MKRIIFNFCF VWLAVSAFAG SKVVEMRNYG LVPDTHENLS PKLQKALQDI KSQVALGDKV
     TLLFESGRYD FHPEGAAVRE YYISNHDQDN PKTVGFPLED WKGLTVDGQG ADFIFHGRML
     PLSLLRSENC TLRNFSIDFE TPHIAQVKIL ESGEEGITFE PAAWVKCRIN EKGFFEAYGE
     GWSSAPQGGI AFEEKTKRLV YRTSDLWCPM EGVKEVSPRV YHAPQWKDAR LKPGTVVALR
     TYYRPAPGIF LSNDKDTRLQ NVKVHYAEGM GLLAQLCENI TLDEFSVCLR GDKDPRYFTT
     QADATHFSSC RGKIDSRNGL YEGMMDDAIN VHGTYLKIKQ RLDDHTVIAR YMHPQAYGFE
     WGVNGDEVQF VRSATMELTG GKNRVKEILP NDKDTVKGAK EYRITFAEPL DAEITDKEGF
     GIENLSWCPE VYFADNVIRN NRARGTLFST PLKTVVERNL FDHTSGTAIL LCGDCNGWFE
     TGACRNVLIR NNRFINALTN MFQFTEAVIS IYPEIPDLEH QKKYFHGGKG EKGVVIEDNY
     FETFDRPVLF AKSIDGLIFK NNVIRQNTDY PAFHHNKSRF RLLHTRNVKI EKNNFEDGDE
     SIARE