ID   GLAB_AKKM8              Reviewed;         794 AA.
AC   B2UNU8;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 63.
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 B;
DE            EC=3.2.1.22 {ECO:0000250|UniProtKB:Q5LGZ8};
DE   Flags: Precursor;
GN   Name=glaB; OrderedLocusNames=Amuc_0480;
OS   Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC
OS   81048 / CCUG 64013 / CIP 107961 / Muc).
OC   Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales;
OC   Akkermansiaceae; Akkermansia.
OX   NCBI_TaxID=349741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP
RC   107961 / Muc;
RX   PubMed=21390229; DOI=10.1371/journal.pone.0016876;
RA   van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M.,
RA   Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.;
RT   "The genome of Akkermansia muciniphila, a dedicated intestinal mucin
RT   degrader, and its use in exploring intestinal metagenomes.";
RL   PLoS ONE 6:E16876-E16876(2011).
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}.
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DR   EMBL; CP001071; ACD04318.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2UNU8; -.
DR   SMR; B2UNU8; -.
DR   STRING; 349741.Amuc_0480; -.
DR   CAZy; CBM51; Carbohydrate-Binding Module Family 51.
DR   CAZy; GH110; Glycoside Hydrolase Family 110.
DR   EnsemblBacteria; ACD04318; ACD04318; Amuc_0480.
DR   KEGG; amu:Amuc_0480; -.
DR   eggNOG; COG5434; Bacteria.
DR   HOGENOM; CLU_017693_0_0_0; -.
DR   OMA; ATHFSGC; -.
DR   OrthoDB; 1217730at2; -.
DR   BioCyc; AMUC349741:G1GBX-528-MON; -.
DR   Proteomes; UP000001031; 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; -; 2.
DR   Gene3D; 2.60.120.1060; -; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR013222; Glyco_hyd_98_carb-bd.
DR   InterPro; IPR038637; NPCBM_sf.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   Pfam; PF08305; NPCBM; 1.
DR   SMART; SM00776; NPCBM; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; Reference proteome; Repeat; Signal.
FT   SIGNAL          1..57
FT                   /evidence="ECO:0000255"
FT   CHAIN           58..794
FT                   /note="Alpha-1,3-galactosidase B"
FT                   /id="PRO_0000348475"
FT   REPEAT          468..499
FT                   /note="PbH1 1"
FT   REPEAT          609..631
FT                   /note="PbH1 2"
FT   REPEAT          632..654
FT                   /note="PbH1 3"
FT   REPEAT          665..686
FT                   /note="PbH1 4"
FT   REPEAT          707..728
FT                   /note="PbH1 5"
SQ   SEQUENCE   794 AA;  87763 MW;  CDEF0FFFD10D164A CRC64;
     MEGNLSFSLM EASGRSIFFL IEGIREQSIK NMFSRMFSWS FVVAACLAGL FPAQSQGEEK
     AAQSGTIAVK VPASSLLMTR QETGETRLDR SFSNAGLSIG GKKYATGIGT HATSMIPLPV
     PENPKVLRLE GACGIDDGAD GDGSVEFRVM SGSEVLWSSG VMRRGMAAKK FSIPVAENGI
     RHLYLMADRV DNNSYDHADW VDLAWKTTGS GQGMKGAVVN ASEFGMVPGV RKDQGPALRA
     AVSALRRQGG GVLNIPRGIY HFYPEGALNM SFHISNHDQP LIHPVCVPLA DLRNVRVEGN
     GSLFLFHGKV VPLLVMDSEN VSINRLSVDY ERSWCTEARV VKTDDRFTEV EIDKKAYPYE
     IRNNRFVFQG KGWEEGMGSC MAFEKGTGHI IANTSDIGWN GHVEPLGGSR LRLSWNLRQK
     GIKPGDTLVL RNYNRPHPGC VVYRARKTSL NDVSLHQSSG MALLVQRSED FHMKGGGVMV
     RKGTGRVHTA GADATHFSNT RGGIVVEKAL FEGMMDDAIN VHSTCLGVME VVDSHTLKCK
     YMHRQAVGFE VFLPGEKIRF INGPTLEPGG TATVKTAVKK NSAEMVITVE EPLPSSVRAG
     DAVENADFYP SVVFRNNIVR NNRARGSLFT TPERVLVEGN LFDHSSGSAI LLAGDAQGWY
     ESGACHEVVI RKNTFINNLT SRYQFTNAII SIYPEVKQLD RQRDYYHRNV LIENNVFKTF
     DVPLLFAIST DNLKFINNKV IYNDEFKGWG QKPFQFRRCA NILIKDNKVL PPRTWTLEDC
     KLENTPSDQV RFGG