GENTAUR Molecular Products.

 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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