ID E5X335_9BACE Unreviewed; 778 AA.
AC E5X335;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Glycosyl hydrolase family 2 {ECO:0000313|EMBL:EFV28373.1};
GN ORFNames=HMPREF1016_03342 {ECO:0000313|EMBL:EFV28373.1};
OS Bacteroides eggerthii 1_2_48FAA.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=665953 {ECO:0000313|EMBL:EFV28373.1, ECO:0000313|Proteomes:UP000003246};
RN [1] {ECO:0000313|EMBL:EFV28373.1, ECO:0000313|Proteomes:UP000003246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1_2_48FAA {ECO:0000313|EMBL:EFV28373.1,
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:EFV28373.1}.
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DR EMBL; ACWG01000041; EFV28373.1; -; Genomic_DNA.
DR AlphaFoldDB; E5X335; -.
DR HOGENOM; CLU_006501_0_1_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; 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:EFV28373.1}.
FT DOMAIN 21..171
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 180..284
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 291..521
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 598..657
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 670..766
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
SQ SEQUENCE 778 AA; 88748 MW; 3270659D43A3FF0F CRC64;
MVTAGVVGIF AQGENRLKDN FDFDWKFSLN DDRQYADPVY NDQSWEDIQL PHDWSIKLNF
DHSISGSAAH LPGGIGWYRK AFIVPASYKN KSVSVLFDGI FHQSDVYING KHLGFRPYGF
CSIEYDLTPY LKYGEKNIIS VRVDRSGKDN IARWYTGSGI YRHAWLIVTN PMHVINNGTY
VTTPEIDAQR ACVAVVTSLT NTSHQEETAT LMQYILDKEG KVVAKSDNRK VTVQPKDTVD
VTQQLNLENP VLWSIDTPSM YTMKTIVKIG RKTVDDYRTP FGVRTIEFTA DRGFFLNGQQ
VKLKGLCLHQ DAGALGTAVP DRSSERRLEI LKEYGCNAIR CAHNQPSPEF LDMCDRMGFI
VIDEAFDKWK SGYYAKYFDE WWQKDMEDML LRDRNHPSVV LWSIGNELQE AWESSDEGVE
RAKMLQDFVH QKEPSRMAIL SAQNNHQEKF SGVTDVIGYN YLEARMLSDH KKFPERRFMI
TEELPYYSGE EGNIRSYTPY NPWNIIAENE FVAGGFIWSG VDYLGEAASR ESHGWPNGLF
DICMFEKPRA AYHRAMWNNK PLVSIAFLDP SLDIDHGRDL WQWPKMASHW NLPRTYFGQV
IQVCTITNCE EVEMFMNGKS MGKQKTADFT NNTIIWNIPY RPGTLEAKGY NDGKEVAAYQ
LATSKDTDSL TLTPDRTMIK ADGQDLSHIA IQLYDEDGKP VQTDDKELTV TVEGDGRFLG
IDNGDLRRKN SFSGNRLKTY FGRALVVVQS LRKAGTMTVS VKMEGKATPY VVTIQSVR
//
