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 04-NOV-2026, entry version 111. 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; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales; OC Bacteroidaceae; 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}. 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; AM109957; CAJ33353.1; -; Genomic_DNA. DR EMBL; AE015928; AAO79356.1; -; Genomic_DNA. 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; 226186-BT_4251; -. 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 InParanoid; Q89ZX0; -. DR OMA; AAGKYHC; -. DR OrthoDB; 9807299at2; -. DR Proteomes; UP000001414; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC. DR GO; GO:1990756; F:ubiquitin-like ligase-substrate adaptor activity; IBA:GO_Central. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 3. DR InterPro; IPR057275; Beta-barrel_GLAA-B_I. DR InterPro; IPR056441; Beta-barrel_GLAA-B_II. DR InterPro; IPR039448; Beta_helix. DR InterPro; IPR006626; PbH1. DR InterPro; IPR012334; Pectin_lyas_fold. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR Pfam; PF23763; Beta-barrel_GLAA-B_I; 1. DR Pfam; PF23764; Beta-barrel_GLAA-B_II; 1. DR Pfam; PF13229; Beta_helix; 1. DR SMART; SM00710; PbH1; 6. DR SUPFAM; SSF51126; Pectin lyase-like; 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 //