GH109_SHEON
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 03-AUG-2022, entry version 98.
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; Proteobacteria; 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}.
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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; Q8ECL7; -.
DR KEGG; son:SO_3120; -.
DR PATRIC; fig|211586.12.peg.3020; -.
DR eggNOG; COG0673; Bacteria.
DR HOGENOM; CLU_046965_0_0_6; -.
DR OMA; MESGKHA; -.
DR OrthoDB; 1465613at2; -.
DR BioCyc; SONE211586:G1GMP-2891-MON; -.
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 InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR Pfam; PF10518; TAT_signal; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 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
