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Database: UniProt
Entry: O43097
LinkDB: O43097
Original site: O43097 
ID   XYNA_THELA              Reviewed;         225 AA.
AC   O43097; D1MH26;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   05-DEC-2018, entry version 97.
DE   RecName: Full=Endo-1,4-beta-xylanase;
DE            Short=Xylanase;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase;
DE   Flags: Precursor;
GN   Name=XYNA;
OS   Thermomyces lanuginosus (Humicola lanuginosa).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Thermomyces.
OX   NCBI_TaxID=5541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 5826 / Tsiklinsky;
RX   PubMed=8879171; DOI=10.1016/0168-1656(96)01516-7;
RA   Schlacher A., Holzmann K., Hayn M., Steiner W., Schwab H.;
RT   "Cloning and characterization of the gene for the thermostable
RT   xylanase XynA from Thermomyces lanuginosus.";
RL   J. Biotechnol. 49:211-218(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-225.
RA   Guo R., Zhao N.;
RT   "Expression and characterization of the xylanase gene xynA from
RT   Thermomyces lanuginosus in Pichia pastoris.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 81-89; 154-172 AND 193-225, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND MASS SPECTROMETRY.
RC   STRAIN=SS-8;
RA   Shrivastava S., Deepalakshmi P.D., Shukla P., Mukhopadhyay K.;
RT   "Thermomyces lanuginosus SS-8 endo-beta-1,4-D-xylanase precursor.";
RL   Submitted (JUL-2010) to UniProtKB.
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
RC   STRAIN=DSM 5826 / Tsiklinsky;
RX   PubMed=9753433; DOI=10.1021/bi980864l;
RA   Gruber K., Klintschar G., Hayn M., Schlacher A., Steiner W.,
RA   Kratky C.;
RT   "Thermophilic xylanase from Thermomyces lanuginosus: high-resolution
RT   X-ray structure and modeling studies.";
RL   Biochemistry 37:13475-13485(1998).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in
CC         xylans.; EC=3.2.1.8; Evidence={ECO:0000269|Ref.3};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=2223.3 umol/min/mg enzyme {ECO:0000269|Ref.3};
CC       pH dependence:
CC         Optimum pH is 6.0. {ECO:0000269|Ref.3};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius. Thermostable.
CC         {ECO:0000269|Ref.3};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- INDUCTION: By xylan. {ECO:0000269|Ref.3}.
CC   -!- MASS SPECTROMETRY: Mass=21300; Method=MALDI; Range=32-225;
CC       Evidence={ECO:0000269|Ref.3};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000305}.
DR   EMBL; U35436; AAB94633.1; -; Genomic_DNA.
DR   EMBL; GU166389; ACY69861.1; -; Genomic_DNA.
DR   PDB; 1YNA; X-ray; 1.55 A; A=33-225.
DR   PDBsum; 1YNA; -.
DR   ProteinModelPortal; O43097; -.
DR   SMR; O43097; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   mycoCLAP; XYN11A_THELA; -.
DR   BRENDA; 3.2.1.8; 2711.
DR   UniPathway; UPA00114; -.
DR   EvolutionaryTrace; O43097; -.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.180; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_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; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49899; SSF49899; 1.
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; Carbohydrate metabolism; Direct protein sequencing;
KW   Disulfide bond; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Pyrrolidone carboxylic acid; Signal; Xylan degradation.
FT   SIGNAL        1     31
FT   CHAIN        32    225       Endo-1,4-beta-xylanase.
FT                                /FTId=PRO_0000008012.
FT   DOMAIN       32    222       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    117    117       Nucleophile.
FT   ACT_SITE    209    209       Proton donor.
FT   MOD_RES      32     32       Pyrrolidone carboxylic acid.
FT                                {ECO:0000250|UniProtKB:P36217}.
FT   DISULFID    141    185
FT   CONFLICT    130    130       S -> P (in Ref. 2; ACY69861).
FT                                {ECO:0000305}.
FT   CONFLICT    177    177       T -> A (in Ref. 2; ACY69861).
FT                                {ECO:0000305}.
FT   STRAND       37     41       {ECO:0000244|PDB:1YNA}.
FT   STRAND       44     50       {ECO:0000244|PDB:1YNA}.
FT   STRAND       52     54       {ECO:0000244|PDB:1YNA}.
FT   STRAND       56     60       {ECO:0000244|PDB:1YNA}.
FT   STRAND       65     70       {ECO:0000244|PDB:1YNA}.
FT   STRAND       72     84       {ECO:0000244|PDB:1YNA}.
FT   STRAND       90    112       {ECO:0000244|PDB:1YNA}.
FT   TURN        113    115       {ECO:0000244|PDB:1YNA}.
FT   STRAND      116    127       {ECO:0000244|PDB:1YNA}.
FT   TURN        129    132       {ECO:0000244|PDB:1YNA}.
FT   STRAND      134    141       {ECO:0000244|PDB:1YNA}.
FT   STRAND      144    158       {ECO:0000244|PDB:1YNA}.
FT   STRAND      161    174       {ECO:0000244|PDB:1YNA}.
FT   STRAND      177    182       {ECO:0000244|PDB:1YNA}.
FT   HELIX       183    192       {ECO:0000244|PDB:1YNA}.
FT   STRAND      199    212       {ECO:0000244|PDB:1YNA}.
FT   STRAND      214    223       {ECO:0000244|PDB:1YNA}.
SQ   SEQUENCE   225 AA;  24356 MW;  FAA79A914C5C676C CRC64;
     MVGFTPVALA ALAATGALAF PAGNATELEK RQTTPNSEGW HDGYYYSWWS DGGAQATYTN
     LEGGTYEISW GDGGNLVGGK GWNPGLNARA IHFEGVYQPN GNSYLAVYGW TRNPLVEYYI
     VENFGTYDPS SGATDLGTVE CDGSIYRLGK TTRVNAPSID GTQTFDQYWS VRQDKRTSGT
     VQTGCHFDAW ARAGLNVNGD HYYQIVATEG YFSSGYARIT VADVG
//
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