ID E6WX38_PSEUU Unreviewed; 380 AA.
AC E6WX38;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN OrderedLocusNames=Psesu_2913 {ECO:0000313|EMBL:ADV28737.1};
OS Pseudoxanthomonas suwonensis (strain 11-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=743721 {ECO:0000313|EMBL:ADV28737.1, ECO:0000313|Proteomes:UP000008632};
RN [1] {ECO:0000313|EMBL:ADV28737.1, ECO:0000313|Proteomes:UP000008632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11-1 {ECO:0000313|Proteomes:UP000008632};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Ovchinnikova G., Siebers A.K., Allgaier M., Thelen M.P.,
RA Hugenholtz P., Gladden J., Woyke T.;
RT "Complete sequence of Pseudoxanthomonas suwonensis 11-1.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8; Evidence={ECO:0000256|RuleBase:RU361174};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000256|RuleBase:RU361174}.
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DR EMBL; CP002446; ADV28737.1; -; Genomic_DNA.
DR RefSeq; WP_013536562.1; NC_014924.1.
DR AlphaFoldDB; E6WX38; -.
DR STRING; 743721.Psesu_2913; -.
DR KEGG; psu:Psesu_2913; -.
DR eggNOG; COG3693; Bacteria.
DR HOGENOM; CLU_020161_6_1_6; -.
DR OrthoDB; 9815836at2; -.
DR Proteomes; UP000008632; Chromosome.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR031158; GH10_AS.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00591; GH10_1; 1.
DR PROSITE; PS51760; GH10_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361174};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361174};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361174};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361174};
KW Reference proteome {ECO:0000313|Proteomes:UP000008632};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:ADV28737.1}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..380
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003212523"
FT DOMAIN 20..376
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT ACT_SITE 264
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 380 AA; 42250 MW; D067C4B16B557B7A CRC64;
MIRPRTALLA ALALACGSAL AAPKTLKDAY RDDFLLGTAV NDAIVTGEDA AQQALAVRHF
NAITLENSMK VEVLHPEPGK WDFERADAFV EFGRKHGMFL VGHTLVWHNQ TPAWFFEDAG
GKPAGTEVMR ERLRQYIHTV AGRYAGKVQA WDVVNEQIGE DGQYRDTTWV RAYGGDGDAL
MRDAFRFAAE AAPGTALYYN DFNAWRPEKV AGIVRMVGML KASGIRIDGV GIQGHWGLNY
PALADIEAAI DAYHAAGVEV MVTELDVDVL PLTKEGQIIG QGMLHPQFQL PEFTRFLDPY
RDGLPGEVQQ QLAARYAELF ALFHRKRDKL SRVSVWGVAD DMSWKNGYPI PDRTNYPLLF
DRARQPKPAL DAVLKVPQGR
//
