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Database: UniProt
Entry: A0A1I0Q0R1_9FIRM
LinkDB: A0A1I0Q0R1_9FIRM
Original site: A0A1I0Q0R1_9FIRM 
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
//
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