ID W0RR43_9BACT Unreviewed; 384 AA.
AC W0RR43;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=J421_4511 {ECO:0000313|EMBL:AHG92048.1};
OS Gemmatirosa kalamazoonensis.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatirosa.
OX NCBI_TaxID=861299 {ECO:0000313|EMBL:AHG92048.1, ECO:0000313|Proteomes:UP000019151};
RN [1] {ECO:0000313|EMBL:AHG92048.1, ECO:0000313|Proteomes:UP000019151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBS708 {ECO:0000313|EMBL:AHG92048.1,
RC ECO:0000313|Proteomes:UP000019151};
RX PubMed=24699952;
RA Debruyn J.M., Radosevich M., Wommack K.E., Polson S.W., Hauser L.J.,
RA Fawaz M.N., Korlach J., Tsai Y.C.;
RT "Genome Sequence and Methylome of Soil Bacterium Gemmatirosa
RT kalamazoonensis KBS708T, a Member of the Rarely Cultivated Gemmatimonadetes
RT Phylum.";
RL Genome Announc. 2:e00226-14(2014).
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; CP007128; AHG92048.1; -; Genomic_DNA.
DR AlphaFoldDB; W0RR43; -.
DR STRING; 861299.J421_4511; -.
DR KEGG; gba:J421_4511; -.
DR PATRIC; fig|861299.3.peg.4566; -.
DR eggNOG; COG3693; Bacteria.
DR HOGENOM; CLU_020161_6_1_0; -.
DR InParanoid; W0RR43; -.
DR OrthoDB; 9809277at2; -.
DR Proteomes; UP000019151; 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; 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.
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|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:UP000019151};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..384
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004795865"
FT DOMAIN 29..378
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
SQ SEQUENCE 384 AA; 42500 MW; 4806D86276D913B7 CRC64;
MKTTSSLVRA AWCGALMAAA CGHPSASPSP AAASLKNAFR NDFRIGTAIA PRVFDETDSV
DVRLVKTHFN AITPENVLKW EVVHPRPNEY DFSQSDRYVA FGERNGMFIV GHTLVWHSQT
PRWVFQDSAG QPLTRDALLA RMKDHIEHVM GRYKGRIKGW DVVNEALNED GTMRQSPWYR
IIGDDFVVKA FEYAHAVDPA AELYYNDYNL ATPAKRDGAI ALAKRIRAAG IPVAAINSQD
HHKLDPNVPS VALVDSMFQA IGAAGFHANV TELDVDVLPR PMGGNTADVS ARAQMAAASN
PYTASLPDSV QQQLARRYAA LFAVYEKHRD IIDRVTFWGV TDATSWLNGF PVRGRTNWPL
LFDRQGRPKP AFDAVLAAAR RQAM
//
