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
//
