UniProt: A0A0A2U1J1

Database: UniProt
Entry: A0A0A2U1J1_9BACL

LinkDB:  A0A0A2U1J1_9BACL 
Original site:  A0A0A2U1J1_9BACL

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (6)   
   Pfam (1)   
   PROSITE (3)   
Literature (1)   
   PubMed (1)   
All databases (16)   

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ID   A0A0A2U1J1_9BACL        Unreviewed;       211 AA.
AC   A0A0A2U1J1;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Endo-1,4-beta-xylanase {ECO:0000256|ARBA:ARBA00012590, ECO:0000256|PROSITE-ProRule:PRU01097};
DE            EC=3.2.1.8 {ECO:0000256|ARBA:ARBA00012590, ECO:0000256|PROSITE-ProRule:PRU01097};
GN   ORFNames=P364_0118495 {ECO:0000313|EMBL:KGP80623.1};
OS   Paenibacillus sp. MAEPY2.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1395587 {ECO:0000313|EMBL:KGP80623.1, ECO:0000313|Proteomes:UP000030061};
RN   [1] {ECO:0000313|EMBL:KGP80623.1, ECO:0000313|Proteomes:UP000030061}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAEPY2 {ECO:0000313|EMBL:KGP80623.1,
RC   ECO:0000313|Proteomes:UP000030061};
RX   PubMed=24526641;
RA   Chua P., Yoo H.S., Gan H.M., Lee S.M.;
RT   "Draft Genome Sequences of Two Cellulolytic Paenibacillus sp. Strains,
RT   MAEPY1 and MAEPY2, from Malaysian Landfill Leachate.";
RL   Genome Announc. 2:0-0(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|ARBA:ARBA00000681,
CC         ECO:0000256|PROSITE-ProRule:PRU01097, ECO:0000256|RuleBase:RU362015};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC       {ECO:0000256|ARBA:ARBA00004851, ECO:0000256|PROSITE-ProRule:PRU01097,
CC       ECO:0000256|RuleBase:RU362015}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01097, ECO:0000256|RuleBase:RU362015}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGP80623.1}.
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DR   EMBL; AWUK01000026; KGP80623.1; -; Genomic_DNA.
DR   RefSeq; WP_024631692.1; NZ_AWUK01000026.1.
DR   AlphaFoldDB; A0A0A2U1J1; -.
DR   SMR; A0A0A2U1J1; -.
DR   eggNOG; COG0726; Bacteria.
DR   OrthoDB; 9806342at2; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000030061; Unassembled WGS sequence.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.120.180; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR018208; GH11_AS_1.
DR   InterPro; IPR033119; GH11_AS_2.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   PANTHER; PTHR46828; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR   PANTHER; PTHR46828:SF2; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS00777; GH11_2; 1.
DR   PROSITE; PS51761; GH11_3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|PROSITE-ProRule:PRU01097};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW   ProRule:PRU01097};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01097};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|PROSITE-ProRule:PRU01097}; Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651, ECO:0000256|PROSITE-
KW   ProRule:PRU01097}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..211
FT                   /note="Endo-1,4-beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038828080"
FT   DOMAIN          19..211
FT                   /note="GH11"
FT                   /evidence="ECO:0000259|PROSITE:PS51761"
FT   ACT_SITE        105
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        198
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
SQ   SEQUENCE   211 AA;  22836 MW;  6114A9E944A21172 CRC64;
     MFKFSKKLLT VVLAASMSFG VFAATSSAAT DYWQNWTDGG GTVNAVNGSG GNYSVTWQNT
     GNFVVGKGWN VGSPNRTINY NAGVFAPSGN GYLTLYGWTR NALIEYYVVD SWGTYRPTGT
     FKGTVTSDGG TYDIYTTMRY NAPSIDGTQT FAQYWSVRQS KRATGVNSAI TFSNHVNAWA
     SKGMNLGSSW SYQVLATEGY QSSGSSNVTV W
//

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