ID A0A0L6JJI3_9FIRM Unreviewed; 729 AA.
AC A0A0L6JJI3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
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};
DE Flags: Precursor;
GN ORFNames=Bccel_1108 {ECO:0000313|EMBL:KNY25848.1};
OS Pseudobacteroides cellulosolvens ATCC 35603 = DSM 2933.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Pseudobacteroides.
OX NCBI_TaxID=398512 {ECO:0000313|EMBL:KNY25848.1, ECO:0000313|Proteomes:UP000036923};
RN [1] {ECO:0000313|Proteomes:UP000036923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2933 {ECO:0000313|Proteomes:UP000036923};
RA Dassa B., Utturkar S.M., Klingeman D.M., Hurt R.A., Keller M., Xu J.,
RA Reddy Y.H.K., Borovok I., Grinberg I.R., Lamed R., Zhivin O., Bayer E.A.,
RA Brown S.D.;
RT "Near-Complete Genome Sequence of the Cellulolytic Bacterium Bacteroides
RT (Pseudobacteroides) cellulosolvens ATCC 35603.";
RL Submitted (JUL-2015) 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}.
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:KNY25848.1}.
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DR EMBL; LGTC01000001; KNY25848.1; -; Genomic_DNA.
DR RefSeq; WP_050753147.1; NZ_LGTC01000001.1.
DR AlphaFoldDB; A0A0L6JJI3; -.
DR STRING; 398512.Bccel_1108; -.
DR PATRIC; fig|398512.5.peg.1147; -.
DR eggNOG; COG0726; Bacteria.
DR eggNOG; COG3291; Bacteria.
DR eggNOG; COG5498; Bacteria.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000036923; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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 CDD; cd04084; CBM6_xylanase-like; 2.
DR Gene3D; 2.60.120.180; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR005084; CMB_fam6.
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; IPR033119; GH11_AS_2.
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; PF03422; CBM_6; 2.
DR Pfam; PF00457; Glyco_hydro_11; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR PRINTS; PR00911; GLHYDRLASE11.
DR SMART; SM00606; CBD_IV; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR PROSITE; PS51175; CBM6; 2.
DR PROSITE; PS00776; GH11_1; 1.
DR PROSITE; PS00777; GH11_2; 1.
DR PROSITE; PS51761; GH11_3; 1.
DR PROSITE; PS51677; NODB; 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:UP000036923};
KW 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..729
FT /note="endo-1,4-beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005565868"
FT DOMAIN 31..220
FT /note="GH11"
FT /evidence="ECO:0000259|PROSITE:PS51761"
FT DOMAIN 258..373
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 408..523
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 550..727
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT REGION 212..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 116
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
FT ACT_SITE 207
FT /note="Proton donor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
SQ SEQUENCE 729 AA; 78017 MW; 6C36C3055DC77DA8 CRC64;
MKTKMKVIFS IVMCFTILFT MCPINGQAAT TVTTNQTGTH DGYYYSFWNQ GGGSVAMTLG
SGGNYSVTWS NCTNFTCGKG WKTGSPNRNV SFSGSFNGGN NGYLALYGWT KNPLIEYYVI
ENYGAWTPPG GTSLGTFNSD GGTYNLYKMQ RVNQPSIEGT ATFTQYFSVR TTKRSSGTIT
FSNHINAWKS KGMNMGSTWD YQIMESEGYQ SSGSANITVS EGSGTPNNNN NNNNNNNNNN
NNNNNNNNNN TATKSAFSTI EAESYNATNS STIQVNGGSI GYIESGNTVT YRNVDFGSGA
TSFSAAVASQ QNSNIQIRVG SANGTLLGTL SNVSTGGWDT YQNKSCNINR VTGVQDLVLV
FSGPVNVNSF VFSGGNTNNN NNNNNNNNNN NNNNNNNNNN TAAKSAFSTI EAESYNATNS
STIQVNGGSI GYINSGNTVT YRNIDFGSGA TSFSAAVASQ QNSNIQIRVG SANGTLLGTL
SNVSTGGWDT YQNKSCNINR VTGVQDLVLV FSGPVNVNSF VFSGSNTGSN TNNNTNNNNN
NNSNQNGANG NVYLCFDDGP NNSNSQTLIN NLKSAGCDKA TMFVWGNKIS SNSTGWDAYK
NSGFSLQNHS WSHQHMTSWS YQQVYNDLKQ CSDAIQNAGK PKPTKIRLPY LESNSTIQQA
CSALGLSIVS PTVDTKDWNG ANTQSIISAC NSLQAGGNPL MHDQYQATNQ AVSTIVQNLK
SRGLGFAQY
//
