ID   GLAB_BACTN              Reviewed;         615 AA.
AC   Q89ZX0;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Alpha-1,3-galactosidase B;
DE            EC=3.2.1.n1 {ECO:0000269|PubMed:18227066};
DE            EC=3.2.1.n2 {ECO:0000269|PubMed:18227066};
DE   AltName: Full=BtGal110B;
DE   AltName: Full=Exo-alpha-galactosidase B;
DE            EC=3.2.1.22 {ECO:0000269|PubMed:18227066};
DE   Flags: Precursor;
GN   Name=glaB; OrderedLocusNames=BT_4251;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
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 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
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. 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:0000269|PubMed:18227066};
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: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. B subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AM109957; CAJ33353.1; -; Genomic_DNA.
DR   EMBL; AE015928; AAO79356.1; -; Genomic_DNA.
DR   RefSeq; NP_813162.1; NC_004663.1.
DR   RefSeq; WP_008764450.1; NC_004663.1.
DR   AlphaFoldDB; Q89ZX0; -.
DR   SMR; Q89ZX0; -.
DR   STRING; 226186.BT_4251; -.
DR   CAZy; GH110; Glycoside Hydrolase Family 110.
DR   PaxDb; Q89ZX0; -.
DR   PRIDE; Q89ZX0; -.
DR   DNASU; 1074743; -.
DR   EnsemblBacteria; AAO79356; AAO79356; BT_4251.
DR   GeneID; 60925426; -.
DR   KEGG; bth:BT_4251; -.
DR   PATRIC; fig|226186.12.peg.4322; -.
DR   eggNOG; COG5434; Bacteria.
DR   HOGENOM; CLU_017693_0_0_10; -.
DR   OMA; ATHFSGC; -.
DR   Proteomes; UP000001414; 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..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..615
FT                   /note="Alpha-1,3-galactosidase B"
FT                   /id="PRO_0000348478"
FT   REPEAT          282..313
FT                   /note="PbH1 1"
FT   REPEAT          423..445
FT                   /note="PbH1 2"
FT   REPEAT          446..467
FT                   /note="PbH1 3"
FT   REPEAT          478..500
FT                   /note="PbH1 4"
FT   REPEAT          520..541
FT                   /note="PbH1 5"
FT   REPEAT          543..573
FT                   /note="PbH1 6"
SQ   SEQUENCE   615 AA;  69373 MW;  19DB3A255E32510C CRC64;
     MRTFLSLKTC LLSALLLCVN SIAASKIISV SDFGLKPDSR INAVPFIQKA IDACKQHPGS
     TLVFPKGRYD FWAQHAIEKD YYETNTYDVN PKILAVLLEQ INDLTIDGNG SEFIMHGRMQ
     PFTLDHCRNI TLKNFSVDWE IPLTAQGIVT QSTSEYLEIE IDSHQYPYII ENKRLTFVGE
     GWKSSLWAIM QFDPDTHLVL PNTGDNLGWR SYDATEINPG LIRLSDPKKE ADKFFPAPGT
     VLVLRHSTRD HAGIFIYHSM DTKLENVKLF HTCGLGILSQ YSKNISFNDV HIIPNTSKKR
     VLSGHDDGFH FMGCSGLLKI ENCSWAGLMD DPINIHGTCS RIMEVLSPTR IKCKFMQDMS
     EGMEWGRPDE TIGFIEHKTM RTVATGKMNK FEALNKAEFI IELSVPLPAG VEAGYVIENL
     TCTPDAEIRN CHFGSCRARG LLVSTPGKVI IENNVFESSG SAILIAGDAN AWYESGAVKD
     VLIRNNDFRY PCNSSIYQFC EAVISIDPEI PTPEQKYPYH RNIRIMDNTF HLFDYPILFA
     RSVNGLTFSS NTLIRDTTYQ PYHYRKEGIT LEACKSVVIS NNKIEGDVLG RIVTIEKMKP
     SDVKISKNPF FKLKK