ID   GLAA_BACFR              Reviewed;         605 AA.
AC   Q64MU6;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Alpha-1,3-galactosidase A;
DE            EC=3.2.1.n1;
DE   AltName: Full=Exo-alpha-galactosidase A;
DE            EC=3.2.1.22;
DE   Flags: Precursor;
GN   Name=glaA; OrderedLocusNames=BF4454;
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 that specifically removes branched alpha-
CC       1,3-linked galactose residues present in blood group B antigens. Has no
CC       activity toward linear alpha-1,3-linked galactose residues (By
CC       similarity). {ECO:0000250}.
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   -!- 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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 110 family. A subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AP006841; BAD51191.1; -; Genomic_DNA.
DR   RefSeq; WP_011203704.1; NC_006347.1.
DR   RefSeq; YP_101725.1; NC_006347.1.
DR   AlphaFoldDB; Q64MU6; -.
DR   SMR; Q64MU6; -.
DR   STRING; 295405.BF4454; -.
DR   CAZy; GH110; Glycoside Hydrolase Family 110.
DR   EnsemblBacteria; BAD51191; BAD51191; BF4454.
DR   KEGG; bfr:BF4454; -.
DR   PATRIC; fig|295405.11.peg.4292; -.
DR   HOGENOM; CLU_017693_0_0_10; -.
DR   OMA; HYMHGLG; -.
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; -; 3.
DR   InterPro; IPR039448; Beta_helix.
DR   InterPro; IPR006626; PbH1.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   Pfam; PF13229; Beta_helix; 1.
DR   SMART; SM00710; PbH1; 6.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; Repeat; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..605
FT                   /note="Alpha-1,3-galactosidase A"
FT                   /id="PRO_0000348472"
FT   REPEAT          256..278
FT                   /note="PbH1 1"
FT   REPEAT          312..334
FT                   /note="PbH1 2"
FT   REPEAT          421..443
FT                   /note="PbH1 3"
FT   REPEAT          444..466
FT                   /note="PbH1 4"
FT   REPEAT          477..507
FT                   /note="PbH1 5"
FT   REPEAT          517..547
FT                   /note="PbH1 6"
SQ   SEQUENCE   605 AA;  68152 MW;  828952376EE4BCB7 CRC64;
     MKKYLHILPA CFLFYAAAHA QQKDTVYVTD FGAVPYSYEN CVTQIQAAID ECKRTGAKVL
     SLPEGRYDIW PEGATRKEYY ISNTSTEQEC PSKVKTVGLM LHEIDDLTIE GNGATLMYHG
     KMTTIALEHC NGVRINNLHI DFERPAGSEI QYRKVTGGET EVTLHRDTRY EIVNGKIRLY
     GEGWRSNKNH CIEYDPDTES FTYSQGWNTL SASDAREIAP GIVRFNTPAE FMPKAGNTLT
     VRDIIRDQVG FFILESKNIT LSRLQMHYMH GLGIVSQYTE NITMDRVKCA PRPDSGRLLA
     ASADMMHFSG CKGKVIIDSC YFAGAQDDPV NVHGTNLRAL EKIDAQTLKL RFMHGQSYGF
     NAYFKGDTVA FIRAATMERF ASATVRDVRR ISDRIVEVRF DRDIPTSLEL NHDCVENMTC
     TPEVEIRNSY FTRTSTRGTL VTTPRKVVIE NNTYYKTGMS AILIEADAEG WYESGPVKDV
     LIKGNTFIDC AYNGGPGHAV IAIHPSNKII DAERPVHQNI RIEDNTFRTF DYPVLYAKST
     AGLLFRNNTI VRTETFPAAS GNPYVFYLNG CKKAVIEGTV FKGETPRQSI KTENMKRKDL
     KTTIK