XYNA_THELA
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 25-MAY-2022, entry version 103.
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 xylanase
RT 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 Thermomyces
RT 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., Kratky C.;
RT "Thermophilic xylanase from Thermomyces lanuginosus: high-resolution X-ray
RT structure and modeling studies.";
RL Biochemistry 37:13475-13485(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC 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;
CC Evidence={ECO:0000269|Ref.3};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000305}.
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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 AlphaFoldDB; O43097; -.
DR SMR; O43097; -.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR CLAE; 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
FT /note="Endo-1,4-beta-xylanase"
FT /id="PRO_0000008012"
FT DOMAIN 32..222
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT ACT_SITE 117
FT /note="Nucleophile"
FT ACT_SITE 209
FT /note="Proton donor"
FT MOD_RES 32
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P36217"
FT DISULFID 141..185
FT CONFLICT 130
FT /note="S -> P (in Ref. 2; ACY69861)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="T -> A (in Ref. 2; ACY69861)"
FT /evidence="ECO:0000305"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:1YNA"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:1YNA"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1YNA"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:1YNA"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:1YNA"
FT STRAND 72..84
FT /evidence="ECO:0007829|PDB:1YNA"
FT STRAND 90..112
FT /evidence="ECO:0007829|PDB:1YNA"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:1YNA"
FT STRAND 116..127
FT /evidence="ECO:0007829|PDB:1YNA"
FT TURN 129..132
FT /evidence="ECO:0007829|PDB:1YNA"
FT STRAND 134..141
FT /evidence="ECO:0007829|PDB:1YNA"
FT STRAND 144..158
FT /evidence="ECO:0007829|PDB:1YNA"
FT STRAND 161..174
FT /evidence="ECO:0007829|PDB:1YNA"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:1YNA"
FT HELIX 183..192
FT /evidence="ECO:0007829|PDB:1YNA"
FT STRAND 199..212
FT /evidence="ECO:0007829|PDB:1YNA"
FT STRAND 214..223
FT /evidence="ECO:0007829|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
