ID   GLAA_BACFN              Reviewed;         605 AA.
AC   Q5L7M8; A4Q8G5;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Alpha-1,3-galactosidase A;
DE            EC=3.2.1.n1;
DE   AltName: Full=BfGal110A;
DE   AltName: Full=Exo-alpha-galactosidase A;
DE            EC=3.2.1.22;
DE   Flags: Precursor;
GN   Name=glaA; OrderedLocusNames=BF4251;
OS   Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS   / NCTC 9343 / Onslow).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=272559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=17401360; DOI=10.1038/nbt1298;
RA   Liu Q.P., Sulzenbacher G., Yuan H., Bennett E.P., Pietz G., Saunders K.,
RA   Spence J., Nudelman E., Levery S.B., White T., Neveu J.M., Lane W.S.,
RA   Bourne Y., Olsson M.L., Henrissat B., Clausen H.;
RT   "Bacterial glycosidases for the production of universal red blood cells.";
RL   Nat. Biotechnol. 25:454-464(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow;
RX   PubMed=15746427; DOI=10.1126/science.1107008;
RA   Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA   Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA   Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA   Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA   Barrell B.G., Parkhill J.;
RT   "Extensive DNA inversions in the B. fragilis genome control variable gene
RT   expression.";
RL   Science 307:1463-1465(2005).
RN   [3]
RP   ENZYME ACTIVITY.
RX   PubMed=18227066; DOI=10.1074/jbc.m709020200;
RA   Liu Q.P., Yuan H., Bennett E.P., Levery S.B., Nudelman E., Spence J.,
RA   Pietz G., Saunders K., White T., Olsson M.L., Henrissat B.,
RA   Sulzenbacher G., Clausen H.;
RT   "Identification of a GH110 subfamily of alpha1,3-galactosidases: novel
RT   enzymes for removal of the alpha3Gal xenotransplantation antigen.";
RL   J. Biol. Chem. 283:8545-8554(2008).
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.
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:0000269|PubMed:18227066};
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:0000269|PubMed:18227066};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 110 family. A subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AM109954; CAJ33350.1; -; Genomic_DNA.
DR   EMBL; CR626927; CAH09922.1; -; Genomic_DNA.
DR   RefSeq; WP_010993781.1; NC_003228.3.
DR   AlphaFoldDB; Q5L7M8; -.
DR   SMR; Q5L7M8; -.
DR   STRING; 272559.BF9343_4141; -.
DR   CAZy; GH110; Glycoside Hydrolase Family 110.
DR   EnsemblBacteria; CAH09922; CAH09922; BF9343_4141.
DR   KEGG; bfs:BF9343_4141; -.
DR   eggNOG; COG5434; Bacteria.
DR   HOGENOM; CLU_017693_0_0_10; -.
DR   OMA; HYMHGLG; -.
DR   OrthoDB; 1217730at2; -.
DR   BioCyc; MetaCyc:MON-21425; -.
DR   SABIO-RK; Q5L7M8; -.
DR   Proteomes; UP000006731; 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; Reference proteome; Repeat; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..605
FT                   /note="Alpha-1,3-galactosidase A"
FT                   /id="PRO_0000348471"
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;  68189 MW;  C57F2747FD520F43 CRC64;
     MKKYLHILPA CFLFYAAAHA QQKDTVYVTD FGAVPYSYEN CVTQIQAAID ECKRTGAKVL
     SLPEGRYDIW PEGAIRKEYY ISNTSTEQEC PSKVKTVGLM LHEIDDLTIE GNGATLMYHG
     KMTTIALEHC NGVRINNLHI DFERPAGSEI QYRKVTGGET EVTLHRDTRY EIVNGKIRLY
     GEGWRSNRNH CIEYDPDTES FTYSQGWNTL SASDAREIAP GIVRFNTPAE FMPKAGNTLT
     VRDIIRDQVG LFILESKNIT LSRLQMHYMH GLGIVSQYTE NITMDRVKCA PRPDSGRLLA
     ASADMMHFSG CKGKVIIDSC YFAGAQDDPV NVHGTNLRAL EKIDAQTLKL RFMHGQSYGF
     NAYFKGDTVA FVRAATMERF ASATVRDVRR ISDRIVEVRF DRDIPTSLEL NHDCVENMTC
     TPEVEIRNCY FTRTSTRGTL VTTPRKVVIE NNTYYKTGMS AILIEADAEG WYESGPVKDV
     LIKGNTFIDC AYNGGPGHAV IAIHPSNKII DAERPVHQNI RIEDNTFRTF DYPVLYAKST
     AGLLFRNNTI VRTETFPAVS GNPYVFYLNG CKKAVIEGTV FEGETPRQSI KTENMKRKDL
     KTTIK