ID A0A1I0Q0R1_9FIRM Unreviewed; 327 AA.
AC A0A1I0Q0R1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Glycosyl hydrolases family 43 {ECO:0000313|EMBL:SEW20545.1};
GN ORFNames=SAMN05216413_1571 {ECO:0000313|EMBL:SEW20545.1};
OS Ruminococcaceae bacterium KH2T8.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae.
OX NCBI_TaxID=1855400 {ECO:0000313|EMBL:SEW20545.1, ECO:0000313|Proteomes:UP000198503};
RN [1] {ECO:0000313|EMBL:SEW20545.1, ECO:0000313|Proteomes:UP000198503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH2T8 {ECO:0000313|EMBL:SEW20545.1,
RC ECO:0000313|Proteomes:UP000198503};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; FOIY01000003; SEW20545.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0Q0R1; -.
DR STRING; 1855400.SAMN05216413_1571; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000198503; 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; cd18619; GH43_CoXyl43_like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
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 Reference proteome {ECO:0000313|Proteomes:UP000198503};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT ACT_SITE 36
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 199
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 137
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; 37397 MW; 55980C2C29ED30CC CRC64;
MKKNERKELV TNIYTADPSA HVFNGKIYIY PSHDEDLDIP EDDDGEQYVM KDYHILSMDS
LDSECVDNGV AISETDIPWV SRQLWAPDAV AVNGKYYLVF PAKDKNDIFR IGVAESDSPV
GPFKAHENYV QGSYSIDPAV LLDDDGKIFC YYGGLWGGQL EMWQSGKFNP DEHRPEGDEK
ALGPMFAQFS QDMKTFVTEP KMITILDENG EPLKAKDEDR RYFEGPWMHK FNGKYYLSYS
TGTTHYLCYA ESDKPEGPFT YKGRIMEPVI GWTTHHSIVE IEGEWYLFYH DAKLSGGCSH
KRCVKFTKLN IAADGTIETI HPYDHEK
//