ID   G1092_BACFN             Reviewed;         425 AA.
AC   Q5LGW9; A4Q8G0;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Alpha-N-acetylgalactosaminidase;
DE            EC=3.2.1.49;
DE   AltName: Full=Glycosyl hydrolase family 109 protein;
GN   OrderedLocusNames=BF0874;
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], AND ENZYME ACTIVITY.
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).
CC   -!- FUNCTION: Glycosidase that has specific alpha-N-acetylgalactosaminidase
CC       activity.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of non-reducing alpha-(1->3)-N-acetylgalactosamine
CC         residues from human blood group A and AB mucin glycoproteins,
CC         Forssman hapten and blood group A lacto series glycolipids.;
CC         EC=3.2.1.49; Evidence={ECO:0000269|PubMed:17401360};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC       Note=Binds 1 NAD(+) per subunit. The NAD(+) cannot dissociate.
CC       {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. Glycosyl hydrolase 109
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AM039447; CAJ01379.1; -; Genomic_DNA.
DR   EMBL; CR626927; CAH06617.1; -; Genomic_DNA.
DR   RefSeq; WP_005813119.1; NC_003228.3.
DR   AlphaFoldDB; Q5LGW9; -.
DR   SMR; Q5LGW9; -.
DR   STRING; 272559.BF9343_0836; -.
DR   CAZy; GH109; Glycoside Hydrolase Family 109.
DR   EnsemblBacteria; CAH06617; CAH06617; BF9343_0836.
DR   KEGG; bfs:BF9343_0836; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_046965_0_0_10; -.
DR   OMA; ENCCYDP; -.
DR   OrthoDB; 1465613at2; -.
DR   Proteomes; UP000006731; Chromosome.
DR   GO; GO:0008456; F:alpha-N-acetylgalactosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; NAD; Reference proteome.
FT   CHAIN           1..425
FT                   /note="Alpha-N-acetylgalactosaminidase"
FT                   /id="PRO_0000348547"
FT   BINDING         29..30
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         51
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         99..102
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         119..120
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         194..198
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         211..214
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         211
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         293
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   425 AA;  47952 MW;  FB747658272705FF CRC64;
     MKTPSQTHVL GLAHPPLPMV RLAFIGLGNR GVLTLQRYLQ IEGVEIKALC EIREGNLVKA
     QKILREAGYP QPDGYTGPDG WKRMCERDDI DLVFICTDWL THTPMAVYSM EHGKHVAIEV
     PAAMTVEECW KLVDTAEKTR QHCMMLENCC YDPFALTTLN MAQQGVFGEI THVEGAYIHD
     LRSIYFADES KGGFHNHWGK KYSIEHTGNP YPTHGLGPVC QILNIHRGDR MNYLVSLSSL
     QAGMTEYARK NFGADSPEAR QKYLLGDMNT TLIQTVKGKS IMIQYNVVTP RPYSRLHTVC
     GTKGFAQKYP VPSIALEPDA GSPLEGKALE EIMERYKHPF TATFGTEAHR RNLPNEMNYV
     MDCRLIYCLR NGLPLDMDVY DAAEWSCITE LSEQSVLNGS IPVEIPDFTR GAWKKCHISR
     TSDLY