ID   E5WZG9_9BACE            Unreviewed;      1075 AA.
AC   E5WZG9;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Glycosyl hydrolase family 2 {ECO:0000313|EMBL:EFV29648.1};
GN   ORFNames=HMPREF1016_02030 {ECO:0000313|EMBL:EFV29648.1};
OS   Bacteroides eggerthii 1_2_48FAA.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=665953 {ECO:0000313|EMBL:EFV29648.1, ECO:0000313|Proteomes:UP000003246};
RN   [1] {ECO:0000313|EMBL:EFV29648.1, ECO:0000313|Proteomes:UP000003246}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1_2_48FAA {ECO:0000313|EMBL:EFV29648.1,
RC   ECO:0000313|Proteomes:UP000003246};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q.,
RA   Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA   Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA   Howarth C., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., White J., Yandava C.,
RA   Allen-Vercoe E., Ambrose C., Strauss J., Daigneault M., Haas B.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacteroides eggerthii strain 1_2_48FAA.";
RL   Submitted (OCT-2010) 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:EFV29648.1}.
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DR   EMBL; ACWG01000025; EFV29648.1; -; Genomic_DNA.
DR   RefSeq; WP_004294155.1; NZ_GL622542.1.
DR   AlphaFoldDB; E5WZG9; -.
DR   HOGENOM; CLU_286156_0_0_10; -.
DR   Proteomes; UP000003246; 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; 1.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
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; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EFV29648.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1075
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003202513"
FT   DOMAIN          91..240
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          242..367
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          408..555
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
SQ   SEQUENCE   1075 AA;  122124 MW;  476237D2298DDB81 CRC64;
     MKRNMTLKSL LLVVCALSGN VFGQSTLSNG KLVYNYPFAP SEGIVNRMEK EYRSEVCLNG
     FWDFQPVSLP STYVQGKGVA PELSLPEEKQ WSDIRIKIPS PWNINAFANR NLEGPDHRNY
     PSYPKEWEQV KMAWMRKKVT IPTEWAGQQI KLYFEAVAGA TEVYINKEKV GENFDLFLPF
     SIDITDKVNA GETVEVLVGV RSQSLFEDNS TIGRRIVPAG SMWGYHIAGI WQDVYLLALP
     KVHVEDIFVK PLVSKGILEL EVTVQNNMAK KADLQVQGDI NEWVNLAGTD VNSAPIPVWK
     LGKKVLEVKA VKVSVPANAS TKVVLQVPVS DELRFWTPEC PNLYALLLSL KVKKQNLDVK
     YERFGWREWT LNGTVQCLNG KPYQLRGDSW HFMGIPQMTR RYAWAWFTAI KGMNGNAVRP
     HAQVYPRFYL DIADEMGICV LNETANWASD GGPKLDSELF WKASKEHLTR FVLRDRNHAS
     VFGWSISNEN KPVILHVFNR SELMTPQKKA WEEWRNIVRL NDPTRPWVSS DGEDDGDGIL
     PVTVGHYGDM NSMKRWIEIG KPWGIGEHSM AYYGTPEQVA KYNGERAYES QLGRMEGLAN
     ECYHLLANQR SMDASYSTVF NMAWYSLKPL PLGKKDLTSK PDISRDGVFF TEYKEGVPGV
     QPERVGPYCT TFNPGYDPNL PLYDPWPMYD AMRAANAPKH PAWSSYAEID KKQYEAPEAF
     PSEKYKEIIF IGRKDSKLKG IMDAQGVKFS TKITAPAQMI YIVDGTYDLP AAEKKSMLVN
     LAKGADVWIW GLTPETVDVY NEILPLSVTL DNLKRSSFLP VQKSWIRGLN NSDFYFCELQ
     RADASEYSLK GALVEEGEVL LNACKTDWRA WNKRPEEIKT AGTIRSEYEC TAATPVFVRY
     QNGASCFYIS TLKEFTNSEK GYNTLRAILK NAGIDCQEIE VKSNELFFLR DNQLVFPAAV
     RDKLIKTTMG RTLDIYVFSP RPLNDLLIEP NMPKLTLVVK TKKCQLSIND EVYAAAEKNR
     YEVTYKELPL LQGWNKISIA IGENDKNEFS GSFRCDNRNE FLPSLKASFV NPEAK
//