ID A0A255SNS2_9BACT Unreviewed; 836 AA.
AC A0A255SNS2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Glycoside hydrolase family 2 {ECO:0000313|EMBL:OYP54638.1};
GN ORFNames=CIK99_12675 {ECO:0000313|EMBL:OYP54638.1};
OS Prevotella sp. P5-92.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=2024222 {ECO:0000313|EMBL:OYP54638.1, ECO:0000313|Proteomes:UP000216769};
RN [1] {ECO:0000313|EMBL:OYP54638.1, ECO:0000313|Proteomes:UP000216769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P5-92 {ECO:0000313|EMBL:OYP54638.1,
RC ECO:0000313|Proteomes:UP000216769};
RA Accetto T., Nograsek B., Avgustin G.;
RT "Comparative genomics of non-oral Prevotella species.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OYP54638.1}.
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; NPJG01000124; OYP54638.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255SNS2; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000216769; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR032311; DUF4982.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR040605; Glyco_hydro2_dom5.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR023232; Glyco_hydro_2_AS.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR Pfam; PF16355; DUF4982; 1.
DR Pfam; PF18565; Glyco_hydro2_C5; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OYP54638.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000216769}.
FT DOMAIN 26..175
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 181..298
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 307..613
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 659..719
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 732..832
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
SQ SEQUENCE 836 AA; 94170 MW; 39777F2153F6A311 CRC64;
MKKLLLSIVA MLAVICRSDA RETLNFDKGW RFALADSTQM SQRDFDDSTW RLLNVPHDWA
IEGDFSASAP SGNSGGALPG GVGWYRKTFS VDAADKGKQF YIDFDGVYMN AKVWINGQLL
GQRPYGYSSF RYDLTPHLKF GGENVVAVRV DNSDQPNSRW YSGCGIYRHV WLVKTEKIHV
AHWGTHVVAE GKKVNVSVVV DNMTGTEEKI VVRNKVVDAE GKTVAEAAKT VTLPSASPML
LVYPPKPADK SRSTYHTTLT VKRPQLWSCE RPYTYKVVTT IELKGKVMDA YETVTGFRTF
SFDAAKGFSL NGKQMKINGV CLHHDLGCLG AAINEDALHR QLRILKEMGT NAIRCSHNPP
APELLAMCDT MGLIVMDESF DMWRRRKTKN DYARFFDEWA ERDLTDLVLR DRNHPSILMW
SVGNEVLEQW SSADADNLTA EQANLILNAG HDASTLAHGE EMSVNSILCR NLCNVIRRYD
TSRPITAGCN EPDPNNHLFK SGALDIIGFN YHHEWVKDVP KNFPGKPFIF SESVSALQTR
GFYMMPSDSV YKAPVEWWLP YQDPSFQCSA YDNMHASWSS THEETWDVVK HNDFVGGQFI
WTGFDYIGEP TPYGFPARSS YFGIVDLAGF PKDSYYMYQS EWTDRQVLHL FPHWNWLPGE
EIDMWCYYNN ADEVELFING RSQGVKAKKD SHQYHLMWRV RFEPGEVKAV ARREGKVVAE
QTIRTAGAPA ALRLSADRDA FVNNPNGDSL AFITVEVTDA DGNLCPRAED QIFFEVEGGR
IVGVDNGNPI SMERFKDTKR KAFNGRALCV VATDGGDVTI KAKGYGLSEK SLTIKK
//