ID G1092_SHESM Reviewed; 456 AA.
AC Q0HH61;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Glycosyl hydrolase family 109 protein 2;
DE EC=3.2.1.-;
DE Flags: Precursor;
GN OrderedLocusNames=Shewmr4_2535;
OS Shewanella sp. (strain MR-4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60480;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-4;
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 Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella sp. MR-4.";
RL Submitted (AUG-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000446; ABI39606.1; -; Genomic_DNA.
DR RefSeq; WP_011623287.1; NC_008321.1.
DR AlphaFoldDB; Q0HH61; -.
DR SMR; Q0HH61; -.
DR CAZy; GH109; Glycoside Hydrolase Family 109.
DR KEGG; she:Shewmr4_2535; -.
DR HOGENOM; CLU_046965_0_0_6; -.
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_5000129974"
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; 50745 MW; 7FC30DD0175A2BB3 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 IQGTNGVFGG FPNRIALENG GSGSYHEWDE
NMDSWYAKYD HPLWTRMGKE AEENGGHGGM DFLMCWRMIY CLRNGEALDQ DVYDGAAWSA
VFPLSVASVG DRGNSKDFPD FTRGVWQTAK PLGIVG
//
