ID   GH109_SHEPA             Reviewed;         456 AA.
AC   A8H2K3;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, 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=Spea_1465;
OS   Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=398579;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700345 / ANG-SQ1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S.Z., Manno D., Hawari J., Richardson P.;
RT   "Complete sequence of Shewanella pealeana ATCC 700345.";
RL   Submitted (OCT-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; CP000851; ABV86790.1; -; Genomic_DNA.
DR   RefSeq; WP_012154716.1; NC_009901.1.
DR   AlphaFoldDB; A8H2K3; -.
DR   SMR; A8H2K3; -.
DR   STRING; 398579.Spea_1465; -.
DR   CAZy; GH109; Glycoside Hydrolase Family 109.
DR   EnsemblBacteria; ABV86790; ABV86790; Spea_1465.
DR   KEGG; spl:Spea_1465; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_046965_0_0_6; -.
DR   OMA; MESGKHA; -.
DR   Proteomes; UP000002608; 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   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   SUPFAM; SSF51735; SSF51735; 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..456
FT                   /note="Glycosyl hydrolase family 109 protein"
FT                   /id="PRO_0000348562"
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         153..154
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         211
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         230
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         242..245
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         242
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         324
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   456 AA;  51367 MW;  62A3A150E9C1B3E9 CRC64;
     MKLNRRHFLK TAGLSAAGIL TSQLPLSSAE AVPKKPAAGP SVMGLVVPKM DTVRVGFIGV
     GQRGSGHVKH FCHLDGVEIK AICDTDPQVL DESIQFVTTQ GLPKPAQYTG SEQAYKDLLN
     RDDIDIVIIS TPWEWHAPMA INTMESGKHA FVEVPLALTV DECWQIVDTA ERTQKNCMMM
     ENVNYGRDEL MVLNMVRQGL FGELLHGEAA YIHELRWQMK EIDSKTGSWR TYWHTKRNGN
     LYPTHGLGPV SQYMNINRGD RFDYLTSMSS PALGRGLYAK REFPADHERN QLDYINGDIN
     TSLIKTVKGR TIMVQHDTTT PRPYSRHNLI QGTNGVFAGF PNRIAIEQAG SDSYHKWDMD
     MAKWYAKYDH PLWLQMGQEA ERNGGHGGMD FLMLWRMVYC LRNSEPLDQD VYDGTAWSVV
     NILSQESVNN RSNSVNFPDF TRGAWKTGKP LGIIGT