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Database: UniProt
Entry: A0A2D1U769_9SPHI
LinkDB: A0A2D1U769_9SPHI
Original site: A0A2D1U769_9SPHI 
ID   A0A2D1U769_9SPHI        Unreviewed;       365 AA.
AC   A0A2D1U769;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=CPT03_13590 {ECO:0000313|EMBL:ATP57430.1};
OS   Pedobacter ginsengisoli.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=363852 {ECO:0000313|EMBL:ATP57430.1, ECO:0000313|Proteomes:UP000223749};
RN   [1] {ECO:0000313|EMBL:ATP57430.1, ECO:0000313|Proteomes:UP000223749}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T01R-27 {ECO:0000313|EMBL:ATP57430.1,
RC   ECO:0000313|Proteomes:UP000223749};
RA   Weon H.-Y., Lee S.A., Sang M.K., Song J.;
RT   "Whole genome of Pedobacter ginsengisoli T01R-27 isolated from tomato
RT   rhizosphere.";
RL   Submitted (OCT-2017) 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; CP024091; ATP57430.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D1U769; -.
DR   KEGG; pgs:CPT03_13590; -.
DR   OrthoDB; 1032269at2; -.
DR   Proteomes; UP000223749; 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; IPR031158; GH10_AS.
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; PS00591; GH10_1; 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|ARBA:ARBA00023295, 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:UP000223749};
KW   Xylan degradation {ECO:0000313|EMBL:ATP57430.1}.
FT   DOMAIN          29..365
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
FT   ACT_SITE        270
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ   SEQUENCE   365 AA;  42650 MW;  8CD51198BB2F416D CRC64;
     MNLLYKAITH TLFAIAVLLL PIYVFAQTSG DQRGLKDYYR DYFPMGVAVT AKQLADSAQQ
     NFILTHFNSL TAENAMKMGP IHPKEDLFFW KDADAIVAFA QKHNLKVRGH NLCWHNQTPK
     WIFYDEFGKQ VSKEVLLQRL KDHIYAVVGR YKGQIYAWDV VNEAVSDEPD QLLRNSLWYQ
     ICGEDFIYKA FQYAHEADPK AILFYNDYNT ENPDKRQRIY KLLKKMRNKG VPVHAIGLQA
     HWTFKDPSQE RLESTLKLFA SLGLKIQITE LDVSIYADGN LQDKTVIAPV SILTPEREQQ
     QAEQYSMIFK VFRNYKKCIS GVTFWNLSDK YSWLDNFPVR GRKNYPLLFD TQLKPKKAYW
     NVVKF
//
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