ID A0A0T6BSB5_9BACI Unreviewed; 213 AA.
AC A0A0T6BSB5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=AB447_214370 {ECO:0000313|EMBL:KRT94560.1}, COP00_19170
GN {ECO:0000313|EMBL:ATH94454.1};
OS Bacillus glycinifermentans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1664069 {ECO:0000313|EMBL:KRT94560.1, ECO:0000313|Proteomes:UP000036168};
RN [1] {ECO:0000313|EMBL:KRT94560.1, ECO:0000313|Proteomes:UP000036168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GO-13 {ECO:0000313|EMBL:KRT94560.1,
RC ECO:0000313|Proteomes:UP000036168};
RX PubMed=26297378; DOI=10.1099/ijsem.0.000462;
RA Kim S.J., Dunlap C.A., Kwon S.W., Rooney A.P.;
RT "Bacillus glycinifermentans sp. nov., isolated from fermented soybean
RT paste.";
RL Int. J. Syst. Evol. Microbiol. 65:3586-3590(2015).
RN [2] {ECO:0000313|EMBL:KRT94560.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GO-13 {ECO:0000313|EMBL:KRT94560.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ATH94454.1, ECO:0000313|Proteomes:UP000218414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBN06P03352 {ECO:0000313|EMBL:ATH94454.1,
RC ECO:0000313|Proteomes:UP000218414};
RA Yu W.-S., Do H.-N., Cheong H.-M., Hwang K.-J.;
RT "Whole genome sequencing of Bacillus glycinfermentans NCCP 15922.";
RL Submitted (SEP-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|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}.
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DR EMBL; CP023481; ATH94454.1; -; Genomic_DNA.
DR EMBL; LECW02000006; KRT94560.1; -; Genomic_DNA.
DR RefSeq; WP_048356553.1; NZ_LECW02000006.1.
DR AlphaFoldDB; A0A0T6BSB5; -.
DR STRING; 1664069.BGLY_2200; -.
DR OrthoDB; 9806342at2; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000036168; Unassembled WGS sequence.
DR Proteomes; UP000218414; 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..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..213
FT /note="Endo-1,4-beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013467867"
FT DOMAIN 20..213
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 200
FT /note="Proton donor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
SQ SEQUENCE 213 AA; 23218 MW; 9C3A529F3AFAA922 CRC64;
MFKFKKNLLV GLTAALMSVS LFSATASAAS TDYWQNWTDG GGIVNAVNGS GGNYSVNWSN
TGNFVVGKGW TTGSPSRTIN YNAGVWAPNG NGYLTLYGWT RSPLIEYYVV DSWGTYRPTG
TYKGTVKSDG GTYDIYTTTR YNAPSIEGPS STFTQYWSVR QSKRPTGSNS KITFSNHVKA
WKSHGMNLGS IWSYQVLATE GYQSSGSSNV TVW
//