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Database: UniProt
Entry: P33558
LinkDB: P33558
Original site: P33558 
ID   XYNA2_CLOSR             Reviewed;         512 AA.
AC   P33558;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   05-DEC-2018, entry version 106.
DE   RecName: Full=Endo-1,4-beta-xylanase A;
DE            Short=Xylanase A;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase A;
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], AND PROTEIN SEQUENCE OF 31-40.
RC   STRAIN=F-9;
RX   PubMed=7763496; DOI=10.1271/bbb.57.273;
RA   Sakka K., Kojima Y., Kondo T., Karita S., Ohmiya K., Shimada K.;
RT   "Nucleotide sequence of the Clostridium stercorarium xynA gene
RT   encoding xylanase A: identification of catalytic and cellulose binding
RT   domains.";
RL   Biosci. Biotechnol. Biochem. 57:273-277(1993).
RN   [2]
RP   SEQUENCE REVISION.
RA   Sakka K.;
RL   Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
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       Temperature dependence:
CC         Optimum temperature is 70 degrees Celsius. Thermostable.;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000305}.
DR   EMBL; D13325; BAA02584.1; -; Genomic_DNA.
DR   ProteinModelPortal; P33558; -.
DR   SMR; P33558; -.
DR   CAZy; CBM6; Carbohydrate-Binding Module Family 6.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   mycoCLAP; XYN11A_CLOST; -.
DR   UniPathway; UPA00114; -.
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; -; 2.
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; 2.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SMART; SM00606; CBD_IV; 2.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS51175; CBM6; 2.
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   Calcium; Carbohydrate metabolism; Cellulose degradation;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Metal-binding;
KW   Polysaccharide degradation; Repeat; Signal; Xylan degradation.
FT   SIGNAL        1     30       {ECO:0000255}.
FT   CHAIN        31    512       Endo-1,4-beta-xylanase A.
FT                                /FTId=PRO_0000008002.
FT   DOMAIN       33    228       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   DOMAIN      251    371       CBM6 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00523}.
FT   REPEAT      279    340       1.
FT   DOMAIN      388    508       CBM6 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00523}.
FT   REPEAT      416    477       2.
FT   REGION      279    477       2 X 61 AA approximate repeats.
FT   COMPBIAS    236    244       Pro-rich.
FT   ACT_SITE    124    124       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    215    215       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10063}.
FT   METAL       254    254       Calcium 1. {ECO:0000250}.
FT   METAL       256    256       Calcium 1. {ECO:0000250}.
FT   METAL       276    276       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       366    366       Calcium 1. {ECO:0000250}.
FT   METAL       391    391       Calcium 2. {ECO:0000250}.
FT   METAL       393    393       Calcium 2. {ECO:0000250}.
FT   METAL       413    413       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       503    503       Calcium 2. {ECO:0000250}.
FT   BINDING     271    271       Substrate 1; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   BINDING     280    280       Substrate 1; via amide nitrogen.
FT                                {ECO:0000250}.
FT   BINDING     337    337       Substrate 1. {ECO:0000250}.
FT   BINDING     364    364       Substrate 1. {ECO:0000250}.
FT   BINDING     417    417       Substrate 2; via amide nitrogen.
FT                                {ECO:0000250}.
FT   BINDING     474    474       Substrate 2. {ECO:0000250}.
FT   BINDING     501    501       Substrate 2. {ECO:0000250}.
SQ   SEQUENCE   512 AA;  55843 MW;  1E133CBF4C139305 CRC64;
     MKRKVKKMAA MATSIIMAIM IILHSIPVLA GRIIYDNETG THGGYDYELW KDYGNTIMEL
     NDGGTFSCQW SNIGNALFRK GRKFNSDKTY QELGDIVVEY GCDYNPNGNS YLCVYGWTRN
     PLVEYYIVES WGSWRPPGAT PKGTITQWMA GTYEIYETTR VNQPSIDGTA TFQQYWSVRT
     SKRTSGTISV TEHFKQWERM GMRMGKMYEV ALTVEGYQSS GYANVYKNEI RIGANPTPAP
     SQSPIRRDAF SIIEAEEYNS TNSSTLQVIG TPNNGRGIGY IENGNTVTYS NIDFGSGATG
     FSATVATEVN TSIQIRSDSP TGTLLGTLYV SSTGSWNTYQ TVSTNISKIT GVHDIVLVFS
     GPVNVDNFIF SRSSPVPAPG DNTRDAYSII QAEDYDSSYG PNLQIFSLPG GGSAIGYIEN
     GYSTTYKNID FGDGATSVTA RVATQNATTI QVRLGSPSGT LLGTIYVGST GSFDTYRDVS
     ATISNTAGVK DIVLVFSGPV NVDWFVFSKS GT
//
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