XYNA1_THEST
ID XYNA1_THEST Reviewed; 651 AA.
AC Q8GJ44; Q93AQ5;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Endo-1,4-beta-xylanase A;
DE EC=3.2.1.8;
DE AltName: Full=1,4-beta-D-xylan xylanohydrolase A;
DE AltName: Full=Xylanase 11A;
DE Short=Xyn11A;
DE Flags: Precursor;
GN Name=xynA;
OS Thermoclostridium stercorarium (Clostridium stercorarium).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Thermoclostridium.
OX NCBI_TaxID=1510;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, SUBCELLULAR
RP LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=NCIB 11745;
RX PubMed=15256568; DOI=10.1099/mic.0.27066-0;
RA Adelsberger H., Hertel C., Glawischnig E., Zverlov V.V., Schwarz W.H.;
RT "Enzyme system of Clostridium stercorarium for hydrolysis of arabinoxylan:
RT reconstitution of the in vivo system from recombinant enzymes.";
RL Microbiology 150:2257-2266(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 235-651, AND FUNCTION.
RC STRAIN=NCIB 11745;
RX PubMed=11849546; DOI=10.1046/j.1365-2958.2002.02730.x;
RA Boraston A.B., McLean B.W., Chen G., Li A., Warren R.A.J., Kilburn D.G.;
RT "Co-operative binding of triplicate carbohydrate-binding modules from a
RT thermophilic xylanase.";
RL Mol. Microbiol. 43:187-194(2002).
RN [3] {ECO:0007744|PDB:1NAE, ECO:0007744|PDB:1O8P, ECO:0007744|PDB:1O8S, ECO:0007744|PDB:1OD3}
RP X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 507-651 IN COMPLEXES WITH
RP D-XYLOTRIOSE; CELLOBIOSE; LAMINARIBIOSE AND CALCIUM IONS.
RX PubMed=12634060; DOI=10.1016/s0022-2836(03)00152-9;
RA Boraston A.B., Notenboom V., Warren R.A.J., Kilburn D.G., Rose D.R.,
RA Davies G.;
RT "Structure and ligand binding of carbohydrate-binding module CsCBM6-3
RT reveals similarities with fucose-specific lectins and 'galactose-binding'
RT domains.";
RL J. Mol. Biol. 327:659-669(2003).
RN [4] {ECO:0007744|PDB:1UY1, ECO:0007744|PDB:1UY2, ECO:0007744|PDB:1UY3, ECO:0007744|PDB:1UY4}
RP X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 235-373 IN COMPLEX WITH
RP D-XYLOBIOSE; D-XYLOTRIOSE; D-XYLOTETRAOSE AND CALCIUM IONS.
RX PubMed=15223327; DOI=10.1016/j.jmb.2004.05.038;
RA Lammerts van Bueren A., Boraston A.B.;
RT "Binding sub-site dissection of a carbohydrate-binding module reveals the
RT contribution of entropy to oligosaccharide recognition at 'non-primary'
RT binding subsites.";
RL J. Mol. Biol. 340:869-879(2004).
CC -!- FUNCTION: Endoxylanase that degrades arabinoxylan and glucuronoxylan to
CC xylobiose and xylotriose (in vitro). {ECO:0000269|PubMed:11849546,
CC ECO:0000269|PubMed:15256568}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:15256568};
CC Temperature dependence:
CC Optimum temperature is 75 degrees Celsius. Thermostable.
CC {ECO:0000269|PubMed:15256568};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15256568}.
CC -!- INDUCTION: Up-regulated by growth on xylan.
CC {ECO:0000269|PubMed:15256568}.
CC -!- DOMAIN: XynA is a modular enzyme. The number of CBM6 (carbohydrate
CC binding type-6) domains varies between strains. The polymeric substrate
CC can interact with several of these CBM6 domains.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000305}.
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DR EMBL; AJ508403; CAD48307.1; -; Genomic_DNA.
DR EMBL; AF417638; AAL14106.1; -; Genomic_DNA.
DR PDB; 1NAE; X-ray; 2.05 A; A=507-651.
DR PDB; 1O8P; X-ray; 2.00 A; A=507-651.
DR PDB; 1O8S; X-ray; 1.15 A; A=507-651.
DR PDB; 1OD3; X-ray; 1.00 A; A=507-651.
DR PDB; 1UY1; X-ray; 1.80 A; A=235-373.
DR PDB; 1UY2; X-ray; 1.70 A; A=235-373.
DR PDB; 1UY3; X-ray; 1.89 A; A=235-373.
DR PDB; 1UY4; X-ray; 1.69 A; A=235-373.
DR PDBsum; 1NAE; -.
DR PDBsum; 1O8P; -.
DR PDBsum; 1O8S; -.
DR PDBsum; 1OD3; -.
DR PDBsum; 1UY1; -.
DR PDBsum; 1UY2; -.
DR PDBsum; 1UY3; -.
DR PDBsum; 1UY4; -.
DR AlphaFoldDB; Q8GJ44; -.
DR SMR; Q8GJ44; -.
DR DrugBank; DB03389; alpha-D-Xylopyranose.
DR DrugBank; DB02379; Beta-D-Glucose.
DR CAZy; CBM6; Carbohydrate-Binding Module Family 6.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR CLAE; XYN11B_CLOST; -.
DR BRENDA; 3.2.1.8; 1520.
DR UniPathway; UPA00114; -.
DR EvolutionaryTrace; Q8GJ44; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.120.180; -; 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; IPR001137; Glyco_hydro_11.
DR Pfam; PF03422; CBM_6; 3.
DR Pfam; PF00457; Glyco_hydro_11; 1.
DR PRINTS; PR00911; GLHYDRLASE11.
DR SMART; SM00606; CBD_IV; 3.
DR SUPFAM; SSF49785; SSF49785; 3.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51175; CBM6; 3.
DR PROSITE; PS00776; GH11_1; 1.
DR PROSITE; PS00777; GH11_2; 1.
DR PROSITE; PS51761; GH11_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carbohydrate metabolism; Cellulose degradation;
KW Glycosidase; Hydrolase; Metal-binding; Polysaccharide degradation; Repeat;
KW Secreted; Signal; Xylan degradation.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..651
FT /note="Endo-1,4-beta-xylanase A"
FT /id="PRO_0000236809"
FT DOMAIN 33..227
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT DOMAIN 250..370
FT /note="CBM6 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00523"
FT REPEAT 278..339
FT /note="1"
FT DOMAIN 387..507
FT /note="CBM6 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00523"
FT REPEAT 415..476
FT /note="2"
FT DOMAIN 527..647
FT /note="CBM6 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00523"
FT REPEAT 555..616
FT /note="3"
FT REGION 278..616
FT /note="3 X 61 AA approximate repeats"
FT ACT_SITE 124
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT ACT_SITE 214
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15223327,
FT ECO:0007744|PDB:1UY1, ECO:0007744|PDB:1UY2,
FT ECO:0007744|PDB:1UY3, ECO:0007744|PDB:1UY4"
FT BINDING 255
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15223327,
FT ECO:0007744|PDB:1UY1, ECO:0007744|PDB:1UY2,
FT ECO:0007744|PDB:1UY3, ECO:0007744|PDB:1UY4"
FT BINDING 270
FT /ligand="D-xylotriose"
FT /ligand_id="ChEBI:CHEBI:62783"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15223327,
FT ECO:0007744|PDB:1UY3"
FT BINDING 275
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15223327,
FT ECO:0007744|PDB:1UY1, ECO:0007744|PDB:1UY2,
FT ECO:0007744|PDB:1UY3, ECO:0007744|PDB:1UY4"
FT BINDING 279
FT /ligand="D-xylobiose"
FT /ligand_id="ChEBI:CHEBI:28309"
FT /evidence="ECO:0000269|PubMed:15223327,
FT ECO:0007744|PDB:1UY2"
FT BINDING 279
FT /ligand="D-xylotriose"
FT /ligand_id="ChEBI:CHEBI:62783"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15223327,
FT ECO:0007744|PDB:1UY3"
FT BINDING 336
FT /ligand="D-xylobiose"
FT /ligand_id="ChEBI:CHEBI:28309"
FT /evidence="ECO:0000269|PubMed:15223327,
FT ECO:0007744|PDB:1UY2"
FT BINDING 336
FT /ligand="D-xylotriose"
FT /ligand_id="ChEBI:CHEBI:62783"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15223327,
FT ECO:0007744|PDB:1UY3"
FT BINDING 363
FT /ligand="D-xylobiose"
FT /ligand_id="ChEBI:CHEBI:28309"
FT /evidence="ECO:0000269|PubMed:15223327,
FT ECO:0007744|PDB:1UY2"
FT BINDING 363
FT /ligand="D-xylotriose"
FT /ligand_id="ChEBI:CHEBI:62783"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15223327,
FT ECO:0007744|PDB:1UY2"
FT BINDING 365
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15223327,
FT ECO:0007744|PDB:1UY1, ECO:0007744|PDB:1UY2,
FT ECO:0007744|PDB:1UY3, ECO:0007744|PDB:1UY4"
FT BINDING 530
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12634060,
FT ECO:0007744|PDB:1NAE, ECO:0007744|PDB:1O8P,
FT ECO:0007744|PDB:1O8S, ECO:0007744|PDB:1OD3"
FT BINDING 532
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12634060,
FT ECO:0007744|PDB:1NAE, ECO:0007744|PDB:1O8P,
FT ECO:0007744|PDB:1O8S, ECO:0007744|PDB:1OD3"
FT BINDING 552
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12634060,
FT ECO:0007744|PDB:1NAE, ECO:0007744|PDB:1O8P,
FT ECO:0007744|PDB:1O8S, ECO:0007744|PDB:1OD3"
FT BINDING 556
FT /ligand="D-xylotriose"
FT /ligand_id="ChEBI:CHEBI:62783"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12634060,
FT ECO:0007744|PDB:1NAE"
FT BINDING 613
FT /ligand="D-xylotriose"
FT /ligand_id="ChEBI:CHEBI:62783"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12634060,
FT ECO:0007744|PDB:1NAE"
FT BINDING 640
FT /ligand="D-xylotriose"
FT /ligand_id="ChEBI:CHEBI:62783"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12634060,
FT ECO:0007744|PDB:1NAE"
FT BINDING 642
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12634060,
FT ECO:0007744|PDB:1NAE, ECO:0007744|PDB:1O8P,
FT ECO:0007744|PDB:1O8S, ECO:0007744|PDB:1OD3"
FT CONFLICT 649..651
FT /note="SGT -> FRNLRV (in Ref. 1; CAD48307)"
FT /evidence="ECO:0000305"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:1UY4"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:1UY4"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:1UY4"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:1UY4"
FT STRAND 297..305
FT /evidence="ECO:0007829|PDB:1UY4"
FT STRAND 310..318
FT /evidence="ECO:0007829|PDB:1UY4"
FT STRAND 323..329
FT /evidence="ECO:0007829|PDB:1UY4"
FT STRAND 339..348
FT /evidence="ECO:0007829|PDB:1UY4"
FT STRAND 350..360
FT /evidence="ECO:0007829|PDB:1UY4"
FT STRAND 363..371
FT /evidence="ECO:0007829|PDB:1UY4"
FT STRAND 523..527
FT /evidence="ECO:0007829|PDB:1O8P"
FT STRAND 535..538
FT /evidence="ECO:0007829|PDB:1OD3"
FT STRAND 543..546
FT /evidence="ECO:0007829|PDB:1OD3"
FT STRAND 550..555
FT /evidence="ECO:0007829|PDB:1OD3"
FT STRAND 562..569
FT /evidence="ECO:0007829|PDB:1OD3"
FT STRAND 574..582
FT /evidence="ECO:0007829|PDB:1OD3"
FT STRAND 587..595
FT /evidence="ECO:0007829|PDB:1OD3"
FT STRAND 600..606
FT /evidence="ECO:0007829|PDB:1OD3"
FT STRAND 616..625
FT /evidence="ECO:0007829|PDB:1OD3"
FT STRAND 627..637
FT /evidence="ECO:0007829|PDB:1OD3"
FT STRAND 640..647
FT /evidence="ECO:0007829|PDB:1OD3"
SQ SEQUENCE 651 AA; 70151 MW; 52E501A16F9D1423 CRC64;
MKRKVKKMAA MATSIIMAIM IILHSIPVLA GRIIYDNETG THGGYDYELW KDYGNTIMEL
NDGGTFSCQW SNIGNALFRK GRKFNSDKTY QELGDIVVEY GCDYNPNGNS YLCVYGWTRN
PLVEYYIVES WGSWRPPGAT PKGTITVDGG TYEIYETTRV NQPSIDGTAT FQQYWSVRTS
KRTSGTISVT EHFKQWERMG MRMGKMYEVA LTVEGYQSSG YANVYKNEIR IGANPTPAPS
QSPIRRDAFS IIEAEEYNST NSSTLQVIGT PNNGRGIGYI ENGNTVTYSN IDFGSGATGF
SATVATEVNT SIQIRSDSPT GTLLGTLYVS STGSWNTYQT VSTNISKITG VHDIVLVFSG
PVNVDNFIFS RSSPVPAPGD NTRDAYSIIQ AEDYDSSYGP NLQIFSLPGG GSAIGYIENG
YSTTYNNVNF ANGLSSITAR VATQISTSIQ VRAGGATGTL LGTIYVPSTN SWDSYQNVTA
NLSNITGVHD ITLVFSGPVN VDYFVFTPAN VNSGPTSPVG GTRSAFSNIQ AEDYDSSYGP
NLQIFSLPGG GSAIGYIENG YSTTYKNIDF GDGATSVTAR VATQNATTIQ VRLGSPSGTL
LGTIYVGSTG SFDTYRDVSA TISNTAGVKD IVLVFSGPVN VDWFVFSKSG T
