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Database: UniProt
Entry: Q8GJ44
LinkDB: Q8GJ44
Original site: Q8GJ44 
ID   XYNA1_CLOSR             Reviewed;         651 AA.
AC   Q8GJ44; Q93AQ5;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   05-DEC-2018, entry version 87.
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   Clostridium stercorarium.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales;
OC   Hungateiclostridiaceae; 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
RT   arabinoxylan: reconstitution of the in vivo system from recombinant
RT   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.,
RA   Kilburn D.G.;
RT   "Co-operative binding of triplicate carbohydrate-binding modules from
RT   a thermophilic xylanase.";
RL   Mol. Microbiol. 43:187-194(2002).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 507-651 IN COMPLEX WITH
RP   SUBSTRATE 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-
RT   binding' domains.";
RL   J. Mol. Biol. 327:659-669(2003).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 235-373 IN COMPLEX WITH
RP   SUBSTRATE AND CALCIUM IONS.
RA   Van Bueren A.L., Boraston A.B.;
RT   "Binding sub-site dissection of a family 6 carbohydrate-binding module
RT   by X-ray crystallography and isothermal titration.";
RL   Submitted (JUN-2004) to the PDB data bank.
CC   -!- FUNCTION: Endoxylanase that degrades arabinoxylan and
CC       glucuronoxylan to xylobiose and xylotriose (in vitro).
CC       {ECO:0000269|PubMed:11849546, ECO:0000269|PubMed:15256568}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in
CC         xylans.; 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
CC       substrate can interact with several of these CBM6 domains.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000305}.
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   ProteinModelPortal; 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   mycoCLAP; XYN11B_CLOST; -.
DR   PRIDE; Q8GJ44; -.
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   Gene3D; 2.60.120.260; -; 3.
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;
KW   Repeat; Secreted; Signal; Xylan degradation.
FT   SIGNAL        1     30       {ECO:0000255}.
FT   CHAIN        31    651       Endo-1,4-beta-xylanase A.
FT                                /FTId=PRO_0000236809.
FT   DOMAIN       33    227       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   DOMAIN      250    370       CBM6 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00523}.
FT   REPEAT      278    339       1.
FT   DOMAIN      387    507       CBM6 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00523}.
FT   REPEAT      415    476       2.
FT   DOMAIN      527    647       CBM6 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00523}.
FT   REPEAT      555    616       3.
FT   REGION      278    616       3 X 61 AA approximate repeats.
FT   ACT_SITE    124    124       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    214    214       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10063}.
FT   METAL       253    253       Calcium 1.
FT   METAL       255    255       Calcium 1.
FT   METAL       275    275       Calcium 1; via carbonyl oxygen.
FT   METAL       365    365       Calcium 1.
FT   METAL       530    530       Calcium 2.
FT   METAL       532    532       Calcium 2.
FT   METAL       552    552       Calcium 2; via carbonyl oxygen.
FT   METAL       642    642       Calcium 2.
FT   BINDING     270    270       Substrate 1; via carbonyl oxygen.
FT                                {ECO:0000269|PubMed:12634060,
FT                                ECO:0000269|Ref.4}.
FT   BINDING     279    279       Substrate 1; via amide nitrogen.
FT                                {ECO:0000269|PubMed:12634060,
FT                                ECO:0000269|Ref.4}.
FT   BINDING     336    336       Substrate 1.
FT                                {ECO:0000269|PubMed:12634060,
FT                                ECO:0000269|Ref.4}.
FT   BINDING     363    363       Substrate 1.
FT                                {ECO:0000269|PubMed:12634060,
FT                                ECO:0000269|Ref.4}.
FT   BINDING     556    556       Substrate 2; via amide nitrogen.
FT                                {ECO:0000269|PubMed:12634060,
FT                                ECO:0000269|Ref.4}.
FT   BINDING     613    613       Substrate 2.
FT                                {ECO:0000269|PubMed:12634060,
FT                                ECO:0000269|Ref.4}.
FT   BINDING     640    640       Substrate 2.
FT                                {ECO:0000269|PubMed:12634060,
FT                                ECO:0000269|Ref.4}.
FT   CONFLICT    649    651       SGT -> FRNLRV (in Ref. 1; CAD48307).
FT                                {ECO:0000305}.
FT   STRAND      258    260       {ECO:0000244|PDB:1UY4}.
FT   STRAND      266    269       {ECO:0000244|PDB:1UY4}.
FT   STRAND      275    279       {ECO:0000244|PDB:1UY4}.
FT   STRAND      285    292       {ECO:0000244|PDB:1UY4}.
FT   STRAND      297    305       {ECO:0000244|PDB:1UY4}.
FT   STRAND      310    318       {ECO:0000244|PDB:1UY4}.
FT   STRAND      323    329       {ECO:0000244|PDB:1UY4}.
FT   STRAND      339    348       {ECO:0000244|PDB:1UY4}.
FT   STRAND      350    360       {ECO:0000244|PDB:1UY4}.
FT   STRAND      363    371       {ECO:0000244|PDB:1UY4}.
FT   STRAND      523    527       {ECO:0000244|PDB:1O8P}.
FT   STRAND      535    538       {ECO:0000244|PDB:1OD3}.
FT   STRAND      543    546       {ECO:0000244|PDB:1OD3}.
FT   STRAND      550    555       {ECO:0000244|PDB:1OD3}.
FT   STRAND      562    569       {ECO:0000244|PDB:1OD3}.
FT   STRAND      574    582       {ECO:0000244|PDB:1OD3}.
FT   STRAND      587    595       {ECO:0000244|PDB:1OD3}.
FT   STRAND      600    606       {ECO:0000244|PDB:1OD3}.
FT   STRAND      616    625       {ECO:0000244|PDB:1OD3}.
FT   STRAND      627    637       {ECO:0000244|PDB:1OD3}.
FT   STRAND      640    647       {ECO:0000244|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
//
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