GLAB_BACFN
ID GLAB_BACFN Reviewed; 595 AA.
AC Q5LGZ8; A4Q8G6;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Alpha-1,3-galactosidase B;
DE EC=3.2.1.n1 {ECO:0000269|PubMed:17401360};
DE EC=3.2.1.n2 {ECO:0000269|PubMed:17401360};
DE AltName: Full=BfGal110B;
DE AltName: Full=Exo-alpha-galactosidase B;
DE EC=3.2.1.22 {ECO:0000269|PubMed:17401360};
DE Flags: Precursor;
GN Name=glaB; Synonyms=fragA; OrderedLocusNames=BF0845;
OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS / NCTC 9343 / Onslow).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=272559;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
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 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow;
RX PubMed=15746427; DOI=10.1126/science.1107008;
RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA Barrell B.G., Parkhill J.;
RT "Extensive DNA inversions in the B. fragilis genome control variable gene
RT expression.";
RL Science 307:1463-1465(2005).
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:0000269|PubMed:17401360}.
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:17401360};
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:17401360};
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:17401360};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.7 mM for Galalpha-pNP {ECO:0000269|PubMed:17401360};
CC pH dependence:
CC Optimum pH is 5-7.5. {ECO:0000269|PubMed:17401360};
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; AM109955; CAJ33351.1; -; Genomic_DNA.
DR EMBL; CR626927; CAH06588.1; -; Genomic_DNA.
DR RefSeq; WP_010992217.1; NC_003228.3.
DR AlphaFoldDB; Q5LGZ8; -.
DR SMR; Q5LGZ8; -.
DR STRING; 272559.BF9343_0807; -.
DR CAZy; GH110; Glycoside Hydrolase Family 110.
DR EnsemblBacteria; CAH06588; CAH06588; BF9343_0807.
DR KEGG; bfs:BF9343_0807; -.
DR eggNOG; COG5434; Bacteria.
DR HOGENOM; CLU_017693_0_0_10; -.
DR OMA; ATHFSGC; -.
DR OrthoDB; 1217730at2; -.
DR BioCyc; MetaCyc:MON-21426; -.
DR SABIO-RK; Q5LGZ8; -.
DR Proteomes; UP000006731; 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 InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 1: Evidence at protein level;
KW Glycosidase; Hydrolase; Reference proteome; Repeat; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..595
FT /note="Alpha-1,3-galactosidase B"
FT /id="PRO_0000348476"
FT REPEAT 432..454
FT /note="PbH1 1"
FT REPEAT 455..477
FT /note="PbH1 2"
FT REPEAT 488..541
FT /note="PbH1 3"
SQ SEQUENCE 595 AA; 67011 MW; F5EE6940D35877A5 CRC64;
MKTILLFALS LLLSLSVSDV CAQERVYDIS QFGLKANSKK NASPVVRKAI AKIKAECRDG
EKVILRFPAG RYNFHEAGST VREYYISNHD QDNPKKVGIA LEDMKNLTID GQGSEFVFYG
RMIPVSLLRS ENCVLKNFSI DFEQPHIAQV QVVENDPEKG ITFEPAPWVD YRISKDSVFE
GLGEGWVMRY SWGIAFDGKT KHVVYNTSDI GCPTKGAFEV APRRICSPKW KDARLVPGTV
VAMRGWGRPT PGIFMSHDVN TSLLDVKVHY AEGMGLLAQL CEDITLDGFG VCLKGDNDPR
YFTTQADATH FSGCKGKIVS KNGLYEGMMD DAINVHGTYL KVIKRVDDHT LIGRYMHDQS
WGFEWGRPGD DVQFVRSETM ELIGKQNQIT AIRPYDKGEI RGAREFSITF KEAIDPAINE
KSGFGIENLT WTPEVLFAGN TIRNNRARGT LFSTPKKTVV EDNLFDHTSG TAILLCGDCN
GWFETGACRD VTIRRNRFIN ALTNMFQFTN AVISIYPEIP NLKDQQKYFH GGKDGGIVIE
DNEFDTFDAP ILYAKSVDGL IFRNNVIKTN TEFKPFHWNK DRFLLERVTN VKISE
