ID E9SA77_RUMAL Unreviewed; 682 AA.
AC E9SA77;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
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 Name=xyn11E {ECO:0000313|EMBL:AEE64770.1};
GN ORFNames=CUS_6528 {ECO:0000313|EMBL:EGC03826.1};
OS Ruminococcus albus 8.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=246199 {ECO:0000313|EMBL:EGC03826.1, ECO:0000313|Proteomes:UP000004259};
RN [1] {ECO:0000313|EMBL:AEE64770.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=8 {ECO:0000313|EMBL:AEE64770.1};
RX PubMed=21666020; DOI=10.1128/AEM.00353-11;
RA Moon Y.H., Iakiviak M., Bauer S., Mackie R.I., Cann I.K.;
RT "Biochemical Analyses of Multiple Endoxylanases from the Rumen Bacterium
RT Ruminococcus albus 8 and Their Synergistic Activities with Accessory
RT Hemicellulose-Degrading Enzymes.";
RL Appl. Environ. Microbiol. 77:5157-5169(2011).
RN [2] {ECO:0000313|EMBL:EGC03826.1, ECO:0000313|Proteomes:UP000004259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8 {ECO:0000313|EMBL:EGC03826.1,
RC ECO:0000313|Proteomes:UP000004259};
RA Nelson K.E., Sutton G., Torralba M., Durkin S., Harkins D., Montgomery R.,
RA Ziemer C., Klaassens E., Ocuiv P., Morrison M.;
RL Submitted (FEB-2011) 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};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC {ECO:0000256|ARBA:ARBA00004851, ECO:0000256|PROSITE-ProRule:PRU01097}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000256|PROSITE-ProRule:PRU01097}.
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DR EMBL; JF314319; AEE64770.1; -; Genomic_DNA.
DR EMBL; ADKM02000050; EGC03826.1; -; Genomic_DNA.
DR RefSeq; WP_002847764.1; NZ_JAJFOM010000001.1.
DR AlphaFoldDB; E9SA77; -.
DR STRING; 246199.CUS_6528; -.
DR eggNOG; COG0726; Bacteria.
DR OrthoDB; 9806342at2; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000004259; Unassembled WGS sequence.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.120.180; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013319; GH11/12.
DR InterPro; IPR018208; GH11_AS_1.
DR InterPro; IPR033123; GH11_dom.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR001137; Glyco_hydro_11.
DR InterPro; IPR002509; NODB_dom.
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; PF02018; CBM_4_9; 1.
DR Pfam; PF00457; Glyco_hydro_11; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR PRINTS; PR00911; GLHYDRLASE11.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR PROSITE; PS00776; GH11_1; 1.
DR PROSITE; PS51761; GH11_3; 1.
DR PROSITE; PS51677; NODB; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000004259};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651, ECO:0000256|PROSITE-
KW ProRule:PRU01097}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..682
FT /note="endo-1,4-beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038284122"
FT DOMAIN 60..261
FT /note="GH11"
FT /evidence="ECO:0000259|PROSITE:PS51761"
FT DOMAIN 476..659
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT REGION 29..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 151
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
FT ACT_SITE 248
FT /note="Proton donor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
SQ SEQUENCE 682 AA; 74815 MW; 31832EFBE95FFB58 CRC64;
MGNRLFVRRA ALAAALVCAV GMTAGCGGTA DDDSRSVSAA ETTTRSEGQT ETMTDKEEQV
FTENITGSAD GYDYELWKDN GDTEMTVMDG GKFKCSWDNI NNALFRRGQK FDCTKTYKDL
GNISIKYGVD YQPDGNSYMC VYGWTRDPLV EYYIVETWGS WRPPGATAPL GTVTVDGGTY
DIYKTTRYEQ PSIDGTKTFD QYWSVRQVKP EMNGTKLEGT ISVSKHFDAW EQVGLELGNM
YEVALNIEGY QSKGHAEIYE NELTIDGNYS ADPAPEVTKN EGGGVMPVAG GVGYFTSNFE
DDECSWQARG PSTVIQSGDE SLEGSGSLFV SGRTDNWNGA SIVLDQEIFK AGSAYAFKVH
ALQKSGSDVT MKLTLQYSDD GGDHYDEVAQ KTVPSGKWTV LENSAFTIPA SAVNPILYVE
SPDSLTDFYI DCAESKGDDG EAVESSSGKT DAEYVFEDPV EIKNTADISW IDKDKPMVAI
AFDDGASAAK KDDPAYRIID TIADNGFHAT FFYVGSWIKT EEQVKYAHDK GMETANHTMT
HPYLSELTPA EIRDEYEKCR VKLKGIIGEE PSAMCRLPYL DDGGETAKTL NDAALITCSV
DTGDWNKATA DQIVEKLEKA MNDGSLDGAI VLCHENYATT AEAMERFVPK LKEAGWQVVT
VSEMFAAREK TMMGGTIYRK IG
//
