ID E2N9B8_9BACE Unreviewed; 327 AA.
AC E2N9B8;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Glycosyl hydrolase, family 43 {ECO:0000313|EMBL:EEF91497.1};
GN ORFNames=BACCELL_00863 {ECO:0000313|EMBL:EEF91497.1};
OS Bacteroides cellulosilyticus DSM 14838.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=537012 {ECO:0000313|EMBL:EEF91497.1, ECO:0000313|Proteomes:UP000003711};
RN [1] {ECO:0000313|EMBL:EEF91497.1, ECO:0000313|Proteomes:UP000003711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14838 {ECO:0000313|EMBL:EEF91497.1,
RC ECO:0000313|Proteomes:UP000003711};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEF91497.1, ECO:0000313|Proteomes:UP000003711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14838 {ECO:0000313|EMBL:EEF91497.1,
RC ECO:0000313|Proteomes:UP000003711};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Bacteroides cellulosilyticus (DSM 14838).";
RL Submitted (JAN-2009) 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:EEF91497.1}.
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; ACCH01000079; EEF91497.1; -; Genomic_DNA.
DR RefSeq; WP_007210252.1; NZ_JANSWE010000071.1.
DR AlphaFoldDB; E2N9B8; -.
DR HOGENOM; CLU_048744_0_0_10; -.
DR Proteomes; UP000003711; 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; cd08981; GH43_Bt1873-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF5; ENDO-ARABINASE; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187, ECO:0000313|EMBL:EEF91497.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..327
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003160967"
FT SITE 159
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 327 AA; 37519 MW; E4A7B9E035634BE3 CRC64;
MKKRELLLLL FSLCSVLVSA QQKVPNRFRT NIPLDSIHLS DPCILADKET STYYMTGTGG
LLWKSKDLAR WEGPYRVAET DPDSWMGPKP EIWAAELHEY NGKYYYFATF TNNAIKIDTV
KGNVIPRRAS HILVSDKPDG PYKPMKDPTY LPENMPTLDG TFWVDSDGKP YMIYCHEWLQ
NWNGTMEKIE LKPDLSGSIG KGKILFRASD SPWSREKMED KVLPNRVTDG PWLFRTGTGR
LGMIWTSWVF QDYTQGVAYS ESGTLDGPWI QEKEPITPPN FGHGMLFRTL DGEWMMSVHS
HKDVNGRYIR IPHLFKVDLS GDKLKID
//
