ID GH109_SHEON Reviewed; 459 AA. AC Q8ECL7; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 105. 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; OrderedLocusNames=SO_3120; OS Shewanella oneidensis (strain MR-1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=211586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ENZYME ACTIVITY. RC STRAIN=ATCC 70050; 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=MR-1; RX PubMed=12368813; DOI=10.1038/nbt749; RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C., RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A., RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C., RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R., RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J., RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J., RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V., RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.; RT "Genome sequence of the dissimilatory metal ion-reducing bacterium RT Shewanella oneidensis."; RL Nat. Biotechnol. 20:1118-1123(2002). 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}. 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; AM039445; CAJ01377.1; -; Genomic_DNA. DR EMBL; AE014299; AAN56125.1; -; Genomic_DNA. DR RefSeq; NP_718681.1; NC_004347.2. DR RefSeq; WP_011073016.1; NZ_CP053946.1. DR AlphaFoldDB; Q8ECL7; -. DR SMR; Q8ECL7; -. DR STRING; 211586.SO_3120; -. DR CAZy; GH109; Glycoside Hydrolase Family 109. DR PaxDb; 211586-SO_3120; -. DR KEGG; son:SO_3120; -. DR PATRIC; fig|211586.12.peg.3020; -. DR eggNOG; COG0673; Bacteria. DR HOGENOM; CLU_046965_0_0_6; -. DR OrthoDB; 9792935at2; -. DR BioCyc; SONE211586:G1GMP-2891-MONOMER; -. DR Proteomes; UP000008186; 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 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 Pfam; PF10518; TAT_signal; 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; Reference proteome; Signal. FT SIGNAL 1..31 FT /note="Tat-type signal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648" FT CHAIN 32..459 FT /note="Alpha-N-acetylgalactosaminidase" FT /id="PRO_0000348561" FT BINDING 64..65 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 86 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 135..138 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 155..156 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 184 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 213 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 232 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 244..247 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 244 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 326 FT /ligand="substrate" FT /evidence="ECO:0000250" SQ SEQUENCE 459 AA; 51965 MW; 4567186636917ADF CRC64; MHNIHRRHFL KAAGAVTAGL VTANIALNAN ASSVAPKPSS GKSVIGLIAP KMEVVRVGFI GVGERGFSHV EQFCHLEGVE LKAICDTHQA VVDRAVEHIV KQKRPKPAVY TGNDLSYREL LNRDDIDIVI ISTPWEWHAP MAIDTMESGK HAFVEVPLAL TVEECWQIID TAERTQKNCM MMENVNYGRE ELMVLNMVRQ GLFGELLHGE AAYIHELRWQ MKEINHKTGS WRTYWHTKRN GNLYPTHGLG PVSQYMNINR GDRFDYLTSM SSPALGRALY AKREFPADHE RNQLKYINGD MSTSLIKTVK GRTIMVQHDT TTPRPYSRHN LIQGTNGVFA GFPNRIAVEN DGFGTSYHKW DTDMQKWYDK YDHPLWQRIG KEAEINGGHG GMDFVMLWRM VYCLRNGEAL DQDVYDGASW SVVNILSEQS LNNRSNSVNF PDFTRGAWEH AKPLGIVGA //