GenomeNet

Database: UniProt
Entry: D3EJU7_GEOS4
LinkDB: D3EJU7_GEOS4
Original site: D3EJU7_GEOS4 
ID   D3EJU7_GEOS4            Unreviewed;       212 AA.
AC   D3EJU7;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 70.
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   OrderedLocusNames=GYMC10_3533 {ECO:0000313|EMBL:ACX65770.1};
OS   Geobacillus sp. (strain Y412MC10).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=481743 {ECO:0000313|EMBL:ACX65770.1, ECO:0000313|Proteomes:UP000002381};
RN   [1] {ECO:0000313|Proteomes:UP000002381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y412MC10 {ECO:0000313|Proteomes:UP000002381};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Brumm P., Mead D.;
RT   "Complete sequence of Geobacillus sp. Y412MC10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACX65770.1, ECO:0000313|Proteomes:UP000002381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y412MC10 {ECO:0000313|EMBL:ACX65770.1,
RC   ECO:0000313|Proteomes:UP000002381};
RX   PubMed=23408395; DOI=10.4056/sigs.2605792;
RA   Mead D.A., Lucas S., Copeland A., Lapidus A., Cheng J.F., Bruce D.C.,
RA   Goodwin L.A., Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C.S.,
RA   Tapia R., Land M., Hauser L.J., Chang Y.J., Kyrpides N.C., Ivanova N.N.,
RA   Ovchinnikova G., Woyke T., Brumm C., Hochstein R., Schoenfeld T., Brumm P.;
RT   "Complete Genome Sequence of Paenibacillus strain Y4.12MC10, a Novel
RT   Paenibacillus lautus strain Isolated from Obsidian Hot Spring in
RT   Yellowstone National Park.";
RL   Stand. Genomic Sci. 6:381-400(2012).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001793; ACX65770.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3EJU7; -.
DR   STRING; 481743.GYMC10_3533; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   KEGG; gym:GYMC10_3533; -.
DR   HOGENOM; CLU_052631_3_2_9; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000002381; Chromosome.
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..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..212
FT                   /note="Endo-1,4-beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003042784"
FT   DOMAIN          20..212
FT                   /note="GH11"
FT                   /evidence="ECO:0000259|PROSITE:PS51761"
FT   ACT_SITE        106
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        199
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
SQ   SEQUENCE   212 AA;  23067 MW;  67F6D5FBA3FE3124 CRC64;
     MIIKFSKKVM TLVLAASMSF GLFATTSNAA TDYWQNWTDG GGTVNAVNGS GGNYSVTWQN
     TGNFVVGKGW NTGSPNRTIN YNAGVWAPSG NGYLTLYGWT RNSLIEYYVV DSWGTYRPTG
     THKGTVTSDG GTYDIYTTMR YNAPSIDGTQ TFAQYWSVRQ SKRATGVNSS ITFSNHVNAW
     ASKGMNLGSS WSYQVLATEG YQSSGSSNVT VW
//
DBGET integrated database retrieval system