ID   G1092_SHESA             Reviewed;         456 AA.
AC   A0KYQ9;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Glycosyl hydrolase family 109 protein 2;
DE            EC=3.2.1.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=Shewana3_2701;
OS   Shewanella sp. (strain ANA-3).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=94122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANA-3;
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   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA   Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL   Submitted (SEP-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; CP000469; ABK48928.1; -; Genomic_DNA.
DR   RefSeq; WP_011717585.1; NC_008577.1.
DR   AlphaFoldDB; A0KYQ9; -.
DR   SMR; A0KYQ9; -.
DR   STRING; 94122.Shewana3_2701; -.
DR   CAZy; GH109; Glycoside Hydrolase Family 109.
DR   KEGG; shn:Shewana3_2701; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_046965_0_0_6; -.
DR   OrthoDB; 9792935at2; -.
DR   Proteomes; UP000002589; 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   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..33
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           34..456
FT                   /note="Glycosyl hydrolase family 109 protein 2"
FT                   /id="PRO_0000348564"
FT   BINDING         63..64
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         134..137
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         154..155
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         243..246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         243
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         325
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   456 AA;  50759 MW;  8FC30DD61758B9FE CRC64;
     MSGFDRRSFL KASMVTAAAT ALAACASSER ATGTTPKAAG KSVMGLVVPK MDEVRVGLIG
     VGERGIGFVH HFSRIEGARI TAICDTDTLV LARAEKAINE YGRDKPAYFS KGDHAYRDLL
     NRDDVDIVVI ATPWAWHHPM AKEAMLAGKH AFVEVPMAGT IEELWDLVDT AELTQRNCMM
     MENVCYGRDE LMVLNMVRQG LFGELLHGEA AYIHELRWQM KEIDRKTGSW RTAYHAKYNG
     NLYPTHGLGP VAQYMNINRG DRLDYLTSVS SPSLGRAAYA KREFPADHQR NQLKYIGGDM
     NTSLIKTVKG RSIMVQHDTT TPRPYSRHNL IQGTNGVFAG FPNRIALENG GSGSYHEWDE
     NMDSWYAKYD HPLWTRMGKE AEENGGHGGM DFLMCWRMIY CLRNGEALDQ DVYDGAAWSA
     VFPLSVASVG DRGNSKDFPD FTRGVWQTAK PLGIVG
//