ID E5WZE4_9BACE Unreviewed; 543 AA.
AC E5WZE4;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Glycosyl hydrolase family 43 {ECO:0000313|EMBL:EFV29689.1};
GN ORFNames=HMPREF1016_02071 {ECO:0000313|EMBL:EFV29689.1};
OS Bacteroides eggerthii 1_2_48FAA.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=665953 {ECO:0000313|EMBL:EFV29689.1, ECO:0000313|Proteomes:UP000003246};
RN [1] {ECO:0000313|EMBL:EFV29689.1, ECO:0000313|Proteomes:UP000003246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1_2_48FAA {ECO:0000313|EMBL:EFV29689.1,
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 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:EFV29689.1}.
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DR EMBL; ACWG01000025; EFV29689.1; -; Genomic_DNA.
DR RefSeq; WP_004294184.1; NZ_GL622542.1.
DR AlphaFoldDB; E5WZE4; -.
DR HOGENOM; CLU_016508_1_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:UniProtKB-KW.
DR CDD; cd09001; GH43_FsAxh1-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR041542; GH43_C2.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF13; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G00930)-RELATED; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187}.
FT DOMAIN 326..539
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 27
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 201
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 151
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 543 AA; 61647 MW; ECB2A8C94B22E801 CRC64;
MLCTISVAQP VKEAPIKNPM LWADVPDPDV IRVGDTFYLV STTMHLMPGA PVMASKDLKN
WKTVSYIFDK LTDSPKYDLS FSLPLDQQKG EGVGTVYGRG QWATSLKFHN GKFWALLAPN
EQGAMGDTYI FTAPKAEGPW TIHARMRHFH DATLFFDDDG TPYVFFGTGE MCQLTPDLKG
VVEGSLRHYF QREKEETGLL EGTRVIKHRG TYYAMLISQA YSSGLNRREV CYRTKDLNGK
WEKHVILESD FGGFRHLAQG TIVDTEEGDW YGIMFQDRGG VGRVLTLSPV RWIDGWPMLG
DENYKVPEIM RPYKSGQPAT GIVLPDDFDD TRLGLHWQWN HNPVDQAWSL TERPGFLRLK
TSRVVPNLYL APNTLTQRME GPACSGYICM DLSKMKDGDC AGLAAFNGDS GVLTVKKNGK
KLTLEMSEQK VTLTEREKAV TNVDEKIIET VDITKLVNAK QPKIWLRLDG EFRPGQRGGR
DAANFFYSFD GGQWMQIGTK DYRMVFDYRR FFMGTKFGIF NYATKKTGGY VDVDFFKYQC
EEK
//
