ID A0A089Z254_STRGA Unreviewed; 383 AA.
AC A0A089Z254;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=SGLAU_19615 {ECO:0000313|EMBL:AIR99880.1};
OS Streptomyces glaucescens.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1907 {ECO:0000313|EMBL:AIR99880.1, ECO:0000313|Proteomes:UP000029482};
RN [1] {ECO:0000313|Proteomes:UP000029482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40922 / GLA O {ECO:0000313|Proteomes:UP000029482};
RX PubMed=25499805; DOI=10.1016/j.jbiotec.2014.11.036;
RA Ortseifen V., Winkler A., Albersmeier A., Wendler S., Puhler A.,
RA Kalinowski J., Ruckert C.;
RT "Complete genome sequence of the actinobacterium Streptomyces glaucescens
RT GLA.O (DSM 40922) consisting of a linear chromosome and one linear
RT plasmid.";
RL J. Biotechnol. 194:81-83(2015).
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; CP009438; AIR99880.1; -; Genomic_DNA.
DR RefSeq; WP_043503173.1; NZ_CP009438.1.
DR AlphaFoldDB; A0A089Z254; -.
DR STRING; 1907.SGLAU_19615; -.
DR KEGG; sgu:SGLAU_19615; -.
DR eggNOG; COG3693; Bacteria.
DR HOGENOM; CLU_020161_6_0_11; -.
DR OrthoDB; 9815836at2; -.
DR Proteomes; UP000029482; 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; 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; 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|RuleBase:RU361174, ECO:0000313|EMBL:AIR99880.1};
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:UP000029482};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:AIR99880.1}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..383
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001852448"
FT DOMAIN 81..376
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
SQ SEQUENCE 383 AA; 42835 MW; 6DDBBBED8C0B1893 CRC64;
MRSIRSAGLA LAIAALVLPL ATGVATAEPS GDRHAGPQRG VPHSHAAFDR LRHAAPEGFH
VGTAVAGGGH HLSQPYPDPF TSDKEYRRIL ARQFSSVSPE NQMKWEYIHP ERGRYDFAAA
DAIVGFAERH RQVVRGHTLL WHSQNPEWLE QGDFSAQELR AILREHITTV VGRYAGRIQQ
WDVANEIFDD QGRLRTQDNI WIRELGPGIV ADAFRWAHAA DPQAKLFFND YNVESVNAKS
DAYHALVQDL LKQGVPVHGF SVQAHLSTRY GFPGDLESNL RRFDALGLET AVTELDVRMD
VPEGGRPTAA QERTQADYYR RALSACLAVE GCDSFTIWGF TDKYSWVPVF FEGEGFANVM
TGDFVRKPAF WALRDTLWAA RRG
//
