ID A0A222XD37_9CELL Unreviewed; 378 AA.
AC A0A222XD37;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=CBP52_13325 {ECO:0000313|EMBL:ASR55913.1};
OS Cellulomonas sp. PSBB021.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=2003551 {ECO:0000313|EMBL:ASR55913.1, ECO:0000313|Proteomes:UP000214627};
RN [1] {ECO:0000313|EMBL:ASR55913.1, ECO:0000313|Proteomes:UP000214627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PSBB021 {ECO:0000313|EMBL:ASR55913.1,
RC ECO:0000313|Proteomes:UP000214627};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) 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; CP021430; ASR55913.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A222XD37; -.
DR KEGG; cez:CBP52_13325; -.
DR OrthoDB; 9815836at2; -.
DR Proteomes; UP000214627; Chromosome.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0000272; P:polysaccharide 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.
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}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..37
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 38..378
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039279884"
FT DOMAIN 55..368
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT ACT_SITE 290
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 378 AA; 41078 MW; 8FFFCFC2A30222E4 CRC64;
MSPAVPARPG RSRATVRRAR SRAAVLLPLL LALPLAACSG TSEPGPDATT APAPAPLEPV
LAEIAGGSAL DIGFAVAPER LDEPEYREIV DKHASLVVAE NVMKWETTEA ADDEWDFAEG
DRLAEYARST GKKLYGHTLV WHSQLPAWVK ALDEDAMQEA MEDHVRTQAE HFRGQVFAWD
VVNEAVDEDG SRRSDSPFQA TLGDDYIADA FEVAHEADPD AQLCYNDYDI EGVNAKSDGV
YALVEDLLAR DVPIDCLGIQ GHLTAGKLPD DLQENIQRFV DLGLTVRITE LDIRVETPAS
DEALAQQAED YASVATACLA VEGCLGLTVW GVTDRYSWIP MWFEGFGDAL LWDADYEPKP
AFDALVEAVG KGRPGRTG
//
