ID   GH109_TANFO             Reviewed;         468 AA.
AC   A4Q8G1;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=Alpha-N-acetylgalactosaminidase;
DE            EC=3.2.1.49;
DE   AltName: Full=Glycosyl hydrolase family 109 protein;
DE   Flags: Precursor;
GN   Name=nagA;
OS   Tannerella forsythia (Bacteroides forsythus).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Tannerella.
OX   NCBI_TaxID=28112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ENZYME ACTIVITY.
RC   STRAIN=ATCC 43037 / JCM 10827 / FDC 338 / CIP 105219;
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).
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   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC   -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. Glycosyl hydrolase 109
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AM039448; CAJ01380.1; -; Genomic_DNA.
DR   RefSeq; WP_046825560.1; NZ_VFJI01000001.1.
DR   AlphaFoldDB; A4Q8G1; -.
DR   SMR; A4Q8G1; -.
DR   CAZy; GH109; Glycoside Hydrolase Family 109.
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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR   InterPro; IPR049303; Glyco_hydro_109_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR   PANTHER; PTHR43818; BCDNA.GH03377; 1.
DR   PANTHER; PTHR43818:SF1; GLYCOSYL HYDROLASE FAMILY 109 PROTEIN; 1.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   Pfam; PF21252; Glyco_hydro_109_C; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; NAD; Signal.
FT   SIGNAL          1..30
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           31..468
FT                   /note="Alpha-N-acetylgalactosaminidase"
FT                   /id="PRO_0000348548"
FT   BINDING         62..63
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         133..136
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         154..155
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         243..247
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         248
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         260..263
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         342
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   468 AA;  51923 MW;  582356F5CE376FE2 CRC64;
     MENTRRNFLK KVTAAGIGAA GLAVTDQAMA AVNQPGEAAQ QKKKPAGKSD GMLRFGFIGT
     GSRCQEHINN VLGIQGNKIV AICDIQKGPL EKTLKHIAKF NVPEPKVYTG GEREFEKMLN
     NEEFDCVIIA SPWEWHVPMA VAAMKAGVPY VGVEVSAANT VEECWDLVNV SEATGSHLNI
     LENVCYRRDV MAALRMVREG LFGEMIHGTC GYQHDLRDVK FNDGIHYTYQ EGGELRMGPT
     AYAEAQWRTQ HSVTRNGDIY PTHGIGPVAN CLNINRGNRF LSLTSMATQS RGLHNFVVDK
     GGANHPYAKI HFNLGDIVTS MIKCANGQTV IVTHDTNLPR PYSLGFRIQG TRGLWMNDGN
     HVYVEGQSKP HRWDASDDWF KKYDHKLWST LELKAKEAGH GGMDYIMMYD FIDAIRNKKP
     TPMDCYDAAA WSAISGLSEM SIARGGAVVD FPDFTRGQWI HRQPAFAL
//