GH109_SHESW
ID GH109_SHESW Reviewed; 459 AA.
AC A1RI61;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Glycosyl hydrolase family 109 protein;
DE EC=3.2.1.-;
DE Flags: Precursor;
GN OrderedLocusNames=Sputw3181_1518;
OS Shewanella sp. (strain W3-18-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=351745;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W3-18-1;
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., Lykidis A., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella sp. W3-18-1.";
RL Submitted (DEC-2006) 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; CP000503; ABM24356.1; -; Genomic_DNA.
DR RefSeq; WP_011788857.1; NC_008750.1.
DR AlphaFoldDB; A1RI61; -.
DR SMR; A1RI61; -.
DR CAZy; GH109; Glycoside Hydrolase Family 109.
DR KEGG; shw:Sputw3181_1518; -.
DR HOGENOM; CLU_046965_0_0_6; -.
DR OMA; MESGKHA; -.
DR Proteomes; UP000002597; 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 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_5000203918"
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; 51985 MW; 29C03823D4C4C1FB CRC64;
MHNIHRRHFL KAAGAVTAGL ITANITASTH ANSVAPKPQT GKSVIGLIAP KMDVVRVGFI
GVGERGFSHV EQFCHLEGVE LKAICDTHQA VIDRAVAHIA KQNRPQPTVY TGDDLSYRDL
LSRDDIDIVI ISTPWEWHAP MAIETMESGK HAFVEVPLAL TVEECWQIVD TAERTQKNCM
MMENVNYGRE ELMVLNMVRQ GVFGELLHGE AAYIHELRWQ MKEIDHKTGS WRTYWHTKRN
GNLYPTHGLG PVSQYMNINR GDRFDYLTSM SSPALGRALY AKREFPADHE RNQLKYINGD
INTSLIKTVK GRTIMVQHDT TTPRPYSRHN LIQGTNGVFA GFPNRIAVEH GGFGKSYHEW
DMDMQKWYDK YDHPLWQRIG KEAEINGGHG GMDFVMLWRM IYCLRNGEAL DQDVYDAASW
SVVNILSEQS VNNRSNSVTF PDFTRGAWEH AKPLGIVGA