ID   GLAB_PARD8              Reviewed;         612 AA.
AC   A6LFT2;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=BDI_2833;
OS   Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS   5825 / NCTC 11152).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=435591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 110 family. B subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP000140; ABR44546.1; -; Genomic_DNA.
DR   RefSeq; WP_011967019.1; NC_009615.1.
DR   AlphaFoldDB; A6LFT2; -.
DR   SMR; A6LFT2; -.
DR   STRING; 435591.BDI_2833; -.
DR   CAZy; GH110; Glycoside Hydrolase Family 110.
DR   EnsemblBacteria; ABR44546; ABR44546; BDI_2833.
DR   KEGG; pdi:BDI_2833; -.
DR   PATRIC; fig|435591.13.peg.2802; -.
DR   eggNOG; COG5434; Bacteria.
DR   HOGENOM; CLU_017693_0_0_10; -.
DR   OMA; ATHFSGC; -.
DR   OrthoDB; 1217730at2; -.
DR   BioCyc; PDIS435591:G1G5A-2909-MON; -.
DR   Proteomes; UP000000566; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; -; 1.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   SUPFAM; SSF51126; SSF51126; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Glycosidase; Hydrolase; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Repeat; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           20..612
FT                   /note="Alpha-1,3-galactosidase B"
FT                   /id="PRO_0000348481"
FT   REPEAT          431..453
FT                   /note="PbH1 1"
FT   REPEAT          454..476
FT                   /note="PbH1 2"
FT   REPEAT          487..536
FT                   /note="PbH1 3"
FT   LIPID           20
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           20
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   612 AA;  69565 MW;  D9F7986EB522590C CRC64;
     MKWYLWGAVV LLYSLFGSAC STEWRYDLSA YGLSPVENVD NAPAMARALE QIREKCEENQ
     TIVVTLPKGR YEFYPDSAAE RVYFISNHDQ MNPKKVGLPF EGMKNMVFDG QGSELIFHGR
     MLPVSLLDSR NCVLKNFSID FKHPQISQVK VVENDTVNGG ITFEVAPWVH YEIRDSVFVA
     KGEGWELTPG SGIAFEGDTR HLVYNTSDIP VGVRGLIEVS PRLIKSPRWK DNRLVPGTVI
     AMRSWERPAP GVFLYHDVNT TLENIKVHYA EGMGLLAQMS ENITLDGFSV CLKGADDPRY
     FTTQADATHF SACKGAIISK NGLYEGMMDD AINVHGTYLK VVRRVNDSTL VGRYMHPQSY
     GFEWGRVGDS VQFIHSSTME LIGARNRITA IKAVDQPDYR GAKEFEIRFE NTVNPSIHEG
     SGFGIENLEW TPTVLFSDNL IRNNRARGSL FSTPRQTVVE NNVFDHTSGT AILLCGDCNG
     WFETGACRNV LIRKNKFINS LTNMFQFTNA IISIYPEIPD LASQRKYFHS DIVIDANEFI
     TFDRPLVYAK SVDGLVFTNN IVKQNKEYPA FHWNNYRFYF QRVIHSKIEN NYFDEGFIRE
     RDVLEENNGY DI