ID   GH109_SHEPC             Reviewed;         459 AA.
AC   A4Y8C8;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Glycosyl hydrolase family 109 protein;
DE            EC=3.2.1.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=Sputcn32_2490;
OS   Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=319224;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CN-32 / ATCC BAA-453;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella putrefaciens CN-32.";
RL   Submitted (APR-2007) 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; CP000681; ABP76211.1; -; Genomic_DNA.
DR   RefSeq; WP_011919553.1; NC_009438.1.
DR   AlphaFoldDB; A4Y8C8; -.
DR   SMR; A4Y8C8; -.
DR   STRING; 319224.Sputcn32_2490; -.
DR   CAZy; GH109; Glycoside Hydrolase Family 109.
DR   GeneID; 45042950; -.
DR   KEGG; spc:Sputcn32_2490; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_046965_0_0_6; -.
DR   OMA; MESGKHA; -.
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   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; NAD; Signal.
FT   SIGNAL          1..31
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           32..459
FT                   /note="Glycosyl hydrolase family 109 protein"
FT                   /id="PRO_5000241619"
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;  52042 MW;  8B00B89D40CF57B1 CRC64;
     MHNIHRRHFL KAAGAVTAGL ITANITASTH ANSVAPKPQN GKSVIGLIAP KMDVVRVGFI
     GVGERGFSHV EQFCHLEGVE LKAICDTHQT VIDRAVAHIV KQNRPQPTVY TGDDLSYRDL
     LSRDDIDIVI ISTPWEWHAP MAIETMESGK HAFVEVPLAL TVEECWQIVD TAERTQKNCM
     MMENVNYGRE ELMVLNMVRQ GVFGELLHGE AAYIHELRWQ MKEIDHKTGS WRTYWHTKRN
     GNLYPTHGLG PVSQYMNINR GDRFDYLTSM SSPALGRALY AKREFPADHE RNQLKYINGD
     INTSLIKTVK GRTIMVQHDT TTPRPYSRHN LLQGTNGVFA GFPNRIAVEH GGFGKSYHEW
     DMDMQKWYDK YDHPLWQRIG KEAEINGGHG GMDFVMLWRM VYCLRNGEAL DQDVYDAASW
     SVVNILSEQS VNNRSNSVTF PDFTRGAWEH AKPLGIVGA