ID   GLAB1_PHOV8             Reviewed;         592 AA.
AC   A6KWM0;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 74.
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 B1;
DE            EC=3.2.1.22 {ECO:0000250|UniProtKB:Q5LGZ8};
DE   Flags: Precursor;
GN   Name=glaB1; OrderedLocusNames=BVU_0104;
OS   Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 /
OS   NBRC 14291 / NCTC 11154) (Bacteroides vulgatus).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Phocaeicola.
OX   NCBI_TaxID=435590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / NCTC
RC   11154;
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; CP000139; ABR37834.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6KWM0; -.
DR   SMR; A6KWM0; -.
DR   STRING; 435590.BVU_0104; -.
DR   CAZy; GH110; Glycoside Hydrolase Family 110.
DR   PRIDE; A6KWM0; -.
DR   EnsemblBacteria; ABR37834; ABR37834; BVU_0104.
DR   KEGG; bvu:BVU_0104; -.
DR   eggNOG; COG5434; Bacteria.
DR   HOGENOM; CLU_017693_0_0_10; -.
DR   OMA; ATHFSGC; -.
DR   Proteomes; UP000002861; 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; -; 2.
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..14
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           15..592
FT                   /note="Alpha-1,3-galactosidase B"
FT                   /id="PRO_0000348479"
FT   REPEAT          429..451
FT                   /note="PbH1 1"
FT   REPEAT          452..474
FT                   /note="PbH1 2"
FT   REPEAT          485..538
FT                   /note="PbH1 3"
FT   LIPID           15
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           15
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   592 AA;  66484 MW;  836AB742D340C573 CRC64;
     MKLLSVLSLS LVLSCTTLSA QKVYEISAFG LKANSSKNAS PVLQKALAKI KAEYKEGEKV
     ILRFPEGRYE FHEKGAAVRE YYISNHDQTN PKKVGIALED MKNLTLDGQG SEFVFHGRML
     PVSLLRSENC LLKNFSIDFE NPHIAQVKIV ENDPQDGIVF EPAPWVDYRI AKDSIFEAYG
     EGWTMRHSWG IAFDGDTKHL VYNTSDIGCP TKGASEVAPR RIHAPGWKDA RLVPGTVVAM
     RGWGRPTPGI FLSHDVNTTI ENVKVHYAEG MGLLAQLCEN ITLEKFGVCL KGDADPRYFT
     TQADATHFSG CKGKIVSCNG LYEGMMDDAI NVHGTYLKVV KRVDDRTLVG RYMHGQSWGF
     EWGCPGDEVQ FIRSNTMELV GKQNKIISIR PYDKEQTEGA REFLITFQEP VDQVINEQSG
     FGIENLTWTP EVLFSGNVIR NNRARGSLFS TPRKTIVENN LFDHTSGAAI LLCGDCNGWF
     ETGACRHVII RKNRFVNALT NLFQFTNAVI SIYPEIPDLK GQQQYFHGGP EGGIVIEDNE
     FETFDAPILY AKSVDGLVFR NNTIKLNTEY KPFHPNRNRF WLERVTNVTI AE