ID GH109_SHEB5 Reviewed; 459 AA.
AC A3D6B7;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Glycosyl hydrolase family 109 protein;
DE EC=3.2.1.-;
DE Flags: Precursor;
GN OrderedLocusNames=Sbal_2793;
OS Shewanella baltica (strain OS155 / ATCC BAA-1091).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=325240;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS155 / ATCC BAA-1091;
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 Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brettar I.,
RA Klappenbach J., Konstantinidis K., Rodrigues J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS155.";
RL Submitted (FEB-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; CP000563; ABN62280.1; -; Genomic_DNA.
DR RefSeq; WP_011847211.1; NC_009052.1.
DR AlphaFoldDB; A3D6B7; -.
DR SMR; A3D6B7; -.
DR STRING; 325240.Sbal_2793; -.
DR CAZy; GH109; Glycoside Hydrolase Family 109.
DR KEGG; sbl:Sbal_2793; -.
DR HOGENOM; CLU_046965_0_0_6; -.
DR OrthoDB; 9792935at2; -.
DR Proteomes; UP000001557; 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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR049303; Glyco_hydro_109_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR43818; BCDNA.GH03377; 1.
DR PANTHER; PTHR43818:SF1; GLYCOSYL HYDROLASE FAMILY 109 PROTEIN; 1.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR Pfam; PF21252; Glyco_hydro_109_C; 1.
DR Pfam; PF10518; TAT_signal; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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_5000224660"
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; 51893 MW; 73B38A8DE6ADDFAA CRC64;
MHNIHRRNFL KAAGAATAGL VTANIALNAY ASSVAPKPQA GKSVIGLIAP KMDVVRVGFI
GVGERGFSHV EQFCHLEGVE LKAICDTHQA VLDRAVDHIV KQNRPKPAVY TGNDLSYRDL
LSRDDIDIVI ISTPWEWHAP MAIETMESGK HAFVEVPMAL TVEECWQVVD TAERTQKNCM
MMENVNYGRE ELMVLNMVRQ GVFGELLHGE AAYIHELRWQ MKEIDHKTGS WRTYWHTKRN
GNLYPTHGLG PVSQYMNINR GDRFDYLTSM SSPALGRALY AKREFPADHE RNQLKYINGD
INTSLIKTVK GRTIMVQHDT TTPRPYSRHN LIQGTNGVFA GFPNRIAVEN GGFGQSYHEW
DMDMQKWYDK YDHPLWQRIG KEAEINGGHG GMDFVMLWRM IYCLRNGEAL DQDVYDGASW
SVVNILSEHS LNDRSNSVTF PDFTRGAWQT AKPLGIVGA
//
