ID   GH109_SHEWM             Reviewed;         467 AA.
AC   B1KNF7;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Glycosyl hydrolase family 109 protein;
DE            EC=3.2.1.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=Swoo_1749;
OS   Shewanella woodyi (strain ATCC 51908 / MS32).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=392500;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51908 / MS32;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella woodyi ATCC 51908.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Glycosidase. {ECO:0000250}.
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; CP000961; ACA86034.1; -; Genomic_DNA.
DR   RefSeq; WP_012324380.1; NC_010506.1.
DR   AlphaFoldDB; B1KNF7; -.
DR   SMR; B1KNF7; -.
DR   STRING; 392500.Swoo_1749; -.
DR   CAZy; GH109; Glycoside Hydrolase Family 109.
DR   EnsemblBacteria; ACA86034; ACA86034; Swoo_1749.
DR   KEGG; swd:Swoo_1749; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_046965_0_0_6; -.
DR   OMA; MESGKHA; -.
DR   OrthoDB; 1465613at2; -.
DR   Proteomes; UP000002168; Chromosome.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
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..467
FT                   /note="Glycosyl hydrolase family 109 protein"
FT                   /id="PRO_5000317251"
FT   BINDING         66..67
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         137..140
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         157..158
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         246..249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         328
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   467 AA;  52860 MW;  D07F6FC66EE7FADA CRC64;
     MKNFNRRAFL KAAGATTAGL VTSGLILPAS AQPQKMPPKP SNGKSVMGLI SPKLSTVRVG
     FIGVGQRGYG HVKHFCHLEG VEIKAICDTD PAVLDRAIDF VVEQGLAKPN AYTGSEHTYR
     DMLQRDDIDI AIISTPWQWH APMAIDTMEN DKHAFVEVPL AMSVEECWQI VDTAERTQKN
     CMMMENVNYG RDELMVLNMV RQGVFGELIH GEAAYIHELR WQMKELESKT GSWRTHWHTK
     RNGNLYPTHG LGPVSQYMNI NRGDRFDYLT SMSSPALGRA LYAKREFPAD HERNQLNYIN
     GDMSTSLIKT VKGRTIMVQH DTTTPRPYSR HNLIQGTNGV FAGFPNRIAL EQSPFERDEK
     GGESFHRWDM DMTRWYDKYD HPLWQQMGKE AERNGGHGGM DFLMLWRMVY CLRNAEPLDQ
     DVYDGAAWSV VNILSEESVN NRSNSVTFPD FTRGAWKTGK PLGIVGA