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Database: UniProt
Entry: A0A1P8NHN2_9MICO
LinkDB: A0A1P8NHN2_9MICO
Original site: A0A1P8NHN2_9MICO 
ID   A0A1P8NHN2_9MICO        Unreviewed;       391 AA.
AC   A0A1P8NHN2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=BH708_15070 {ECO:0000313|EMBL:APX33817.1};
OS   Brachybacterium sp. P6-10-X1.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC   Brachybacterium.
OX   NCBI_TaxID=1903186 {ECO:0000313|EMBL:APX33817.1, ECO:0000313|Proteomes:UP000185991};
RN   [1] {ECO:0000313|EMBL:APX33817.1, ECO:0000313|Proteomes:UP000185991}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P6-10-X1 {ECO:0000313|EMBL:APX33817.1,
RC   ECO:0000313|Proteomes:UP000185991};
RA   Zhao B., Liao L., Chen B.;
RT   "Complete genome of Brachybacterium sp. P6-10-X1.";
RL   Submitted (SEP-2016) 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; CP017297; APX33817.1; -; Genomic_DNA.
DR   RefSeq; WP_076809901.1; NZ_CP017297.1.
DR   AlphaFoldDB; A0A1P8NHN2; -.
DR   STRING; 1903186.BH708_15070; -.
DR   KEGG; brx:BH708_15070; -.
DR   OrthoDB; 9815836at2; -.
DR   Proteomes; UP000185991; 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|RuleBase:RU361174};
KW   Glycosidase {ECO:0000256|RuleBase:RU361174, ECO:0000313|EMBL:APX33817.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361174};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361174};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000313|EMBL:APX33817.1}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..391
FT                   /note="Beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013156787"
FT   DOMAIN          74..376
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
FT   REGION          20..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   391 AA;  42720 MW;  C1CE89BCA7E195D1 CRC64;
     MKRRQILTVG AVTAATSLAA GGAASAAPPG NAGPPGNGER TPPGLATKDV LAWAAGREIE
     IGSAVAGGGH HTSQPYPPPF TEDETYRELL GREFTSLSAE NQMKWSYLRP DRDTYAFAAA
     DSIMEFARRH GQVVRGHTLL WHSQNPAWLE EGGFGPEELR TILKDHIDTV VGRYAGHIQQ
     WDVVNEIFTE DGALRESENI WIRELGPGII ADAFRWAHAA DPQARLYVND YNVEGVNAKS
     DAYHALVQDL LADGVPVHGF STQGHLSIRY GFPGGLVENL ERFADLGLET AITELDVRMD
     LPDGAEPTQE QLDEQAEYYR RMTEGALAAD GCTSLTLWGF VDTYSWVPAT FEGQGAATVM
     WADYTRKPAY FAVQDALARA SRRAGHPALR D
//
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