ID E5WTU2_9BACE Unreviewed; 452 AA.
AC E5WTU2;
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 43 {ECO:0000313|EMBL:EFV31764.1};
GN ORFNames=HMPREF1016_00093 {ECO:0000313|EMBL:EFV31764.1};
OS Bacteroides eggerthii 1_2_48FAA.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=665953 {ECO:0000313|EMBL:EFV31764.1, ECO:0000313|Proteomes:UP000003246};
RN [1] {ECO:0000313|EMBL:EFV31764.1, ECO:0000313|Proteomes:UP000003246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1_2_48FAA {ECO:0000313|EMBL:EFV31764.1,
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:EFV31764.1}.
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DR EMBL; ACWG01000001; EFV31764.1; -; Genomic_DNA.
DR AlphaFoldDB; E5WTU2; -.
DR HOGENOM; CLU_009397_11_2_10; -.
DR Proteomes; UP000003246; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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; cd04084; CBM6_xylanase-like; 1.
DR CDD; cd18618; GH43_Xsa43E-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF6; -; 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF03422; CBM_6; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SMART; SM00606; CBD_IV; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS51175; CBM6; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022651};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..452
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003202350"
FT DOMAIN 325..451
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT ACT_SITE 32
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 148
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 452 AA; 50539 MW; B8F4ECA1CA8CDABD CRC64;
MSKNLFLSIC LGICSLPAMA QNPIVQTMYT ADPAPLVHND VLYLYTSHDE DASTWFVMND
WKLYTTTDMV NWTDHGAVLS YKTFSWAKGD AWAMQCVERD GKFYAYVPVT SRATNSAAIG
VAVSDSPYGP FIDPLGKPLV QSKKGDIDPT VFIDDDGQAY LYWGNPFCYY VKLNEDMISY
EGDIVRVPMT EEAFGKREGN VKERPTLYEE GPWLYKRNDL YYLLWAGGPI SEHLGYSTSK
SPLGPWKYGG VLMPTEGRSF TNHPGIVDYK GNTYLFYHSG ALPGGSGFTR SVCVEQVEFN
KNGSIKPLKM TEGIQQGLTT LNPYRKTEAE TIAFSEGVKA AQNTEVGVFV NAMHNNAYTK
VKNVNFRDYG PSKFTARVGT THNGGVTMEI RLDSPQGQLL GTTRVPLTGG DDRWALVTTE
TAKVTGVHDL YFIFKGEKPG RIMYFDYWMF SK
//
