ID G4H8M8_9BACL Unreviewed; 330 AA.
AC G4H8M8;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Xylan 1,4-beta-xylosidase {ECO:0000313|EMBL:EHB68213.1};
DE EC=3.2.1.37 {ECO:0000313|EMBL:EHB68213.1};
GN ORFNames=PaelaDRAFT_0339 {ECO:0000313|EMBL:EHB68213.1};
OS Paenibacillus lactis 154.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=743719 {ECO:0000313|EMBL:EHB68213.1, ECO:0000313|Proteomes:UP000003891};
RN [1] {ECO:0000313|EMBL:EHB68213.1, ECO:0000313|Proteomes:UP000003891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=154 {ECO:0000313|EMBL:EHB68213.1,
RC ECO:0000313|Proteomes:UP000003891};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Siebers A., Thelen M., Hugenholtz P.,
RA Allgaier M., Woyke T.J.;
RT "The draft genome of Paenibacillus lactis 154.";
RL Submitted (SEP-2011) 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; AGIP01000001; EHB68213.1; -; Genomic_DNA.
DR RefSeq; WP_007127515.1; NZ_AGIP01000001.1.
DR AlphaFoldDB; G4H8M8; -.
DR STRING; 743719.PaelaDRAFT_0339; -.
DR PATRIC; fig|743719.3.peg.356; -.
DR eggNOG; COG3507; Bacteria.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000003891; Unassembled WGS sequence.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:UniProtKB-EC.
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 Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT ACT_SITE 40
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 204
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 139
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 330 AA; 37096 MW; 451C19452FE14AAC CRC64;
MTKPVQPNEP IVTHIYTADP SAHVFEGKLY IYPSHDLDHD NTSNDNGDQY DMEDYHVFSL
EDVNAPCVDH GEVLHVKDVP WAQKQMWAPD AAFKNDTYYL YFPARDHEGI FRIGVATSSS
PSGPFTPEPN YIPGSFSIDP AVFVDDDNRA YMYFGGLWGG QLEKWQTGTF VPDAEGPAAD
APALGPRVAE LSDDMLTFKA APQEISIVDE NGKPIPAGDE DRRYFEGPWM HKYNGTYYLS
YSTGSTHKIV YATSQSPTGP FEYKGTILTP VLGWTTHHSI VEFKNKWYLF YHDSSLSGGA
DNKRSVKFTE LKYNEDGTIQ TIDPYGNENR
//
