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Beta-xylanase (EC 3.2.1.8)

 R0CX88_CAUVI            Unreviewed;       356 AA.
R0CX88;
26-JUN-2013, integrated into UniProtKB/TrEMBL.
26-JUN-2013, sequence version 1.
27-SEP-2017, entry version 22.
RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
Flags: Precursor;
ORFNames=OR37_03225 {ECO:0000313|EMBL:ENZ80950.1};
Caulobacter crescentus OR37.
Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
Caulobacteraceae; Caulobacter.
NCBI_TaxID=1292034 {ECO:0000313|EMBL:ENZ80950.1, ECO:0000313|Proteomes:UP000013063};
[1] {ECO:0000313|EMBL:ENZ80950.1, ECO:0000313|Proteomes:UP000013063}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=OR37 {ECO:0000313|EMBL:ENZ80950.1,
ECO:0000313|Proteomes:UP000013063};
PubMed=23792749;
Utturkar S.M., Bollmann A., Brzoska R.M., Klingeman D.M.,
Epstein S.E., Palumbo A.V., Brown S.D.;
"Draft Genome Sequence for Caulobacter sp. Strain OR37, a Bacterium
Tolerant to Heavy Metals.";
Genome Announc. 1:0-0(2013).
-!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-xylosidic
linkages in xylans. {ECO:0000256|RuleBase:RU361174}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F)
family. {ECO:0000256|RuleBase:RU361174}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:ENZ80950.1}.
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EMBL; APMP01000024; ENZ80950.1; -; Genomic_DNA.
RefSeq; WP_004622070.1; NZ_APMP01000024.1.
EnsemblBacteria; ENZ80950; ENZ80950; OR37_03225.
PATRIC; fig|1292034.3.peg.3200; -.
OrthoDB; POG091H0Y2G; -.
Proteomes; UP000013063; Unassembled WGS sequence.
GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
InterPro; IPR001000; GH10.
InterPro; IPR031158; GH10_AS.
InterPro; IPR017853; Glycoside_hydrolase_SF.
Pfam; PF00331; Glyco_hydro_10; 1.
PRINTS; PR00134; GLHYDRLASE10.
SMART; SM00633; Glyco_10; 1.
SUPFAM; SSF51445; SSF51445; 1.
PROSITE; PS00591; GH10_1; 1.
PROSITE; PS51760; GH10_2; 1.
3: Inferred from homology;
Carbohydrate metabolism {ECO:0000313|EMBL:ENZ80950.1};
Complete proteome {ECO:0000313|Proteomes:UP000013063};
Glycosidase {ECO:0000256|RuleBase:RU361174,
ECO:0000313|EMBL:ENZ80950.1};
Hydrolase {ECO:0000256|RuleBase:RU361174,
ECO:0000313|EMBL:ENZ80950.1};
Polysaccharide degradation {ECO:0000313|EMBL:ENZ80950.1};
Signal {ECO:0000256|SAM:SignalP};
Xylan degradation {ECO:0000313|EMBL:ENZ80950.1}.
SIGNAL 1 23 {ECO:0000256|SAM:SignalP}.
CHAIN 24 356 Beta-xylanase. {ECO:0000256|SAM:SignalP}.
/FTId=PRO_5004347353.
DOMAIN 34 353 GH10. {ECO:0000259|PROSITE:PS51760}.
ACT_SITE 267 267 Nucleophile. {ECO:0000256|PROSITE-
ProRule:PRU10061}.
SEQUENCE 356 AA; 39513 MW; BDF87841D770F6D3 CRC64;
MRRLTRRSAI ATALALSACG REAASQPAYP PITDTPLKSI ASTPVGACVQ HAFLQDPAYA
ELFARHYSQL TPEWEMKMEY ILQDDGSFRF DRPDAIADFA RRHGIRLYGT TLVWYDQAMP
AFLRLDGQGK AFANAYRNYI LAVAGRYRGQ AVGWDVVNET VADNGVDLRA SIWTRNLGVD
AHMILAFHHA READPEATLF INDYHLENNP TKRATFLRTV ERLLKAGAPI GGIGTQSHLD
LDVTRPGLCR AAIRELAGFG LPIHVSELDI SLGDKPDFAR LPELLKRQAD LTRELAGAYM
DLPARQRFAF TVWGLRDSDT WLHGPSGQRP SDQPLPFDAA GRPKPMFQAL AETLSA


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