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Database: UniProt
Entry: P26514
LinkDB: P26514
Original site: P26514 
ID   XYNA_STRLI              Reviewed;         477 AA.
AC   P26514; P96464;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   23-MAY-2018, entry version 116.
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=xlnA;
OS   Streptomyces lividans.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 42-92.
RC   STRAIN=66 / 1326;
RX   PubMed=1743521; DOI=10.1016/0378-1119(91)90299-Q;
RA   Shareck F., Roy C., Yaguchi M., Morosoli R., Kluepfel D.;
RT   "Sequences of three genes specifying xylanases in Streptomyces
RT   lividans.";
RL   Gene 107:75-82(1991).
RN   [2]
RP   SEQUENCE REVISION TO 20 AND 140-141.
RA   Shareck F.;
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 42-340.
RX   PubMed=8063693;
RA   Derewenda U., Swenson L., Green R., Wei Y.Y., Morosoli R., Shareck F.,
RA   Kluepfel D., Derewenda Z.S.;
RT   "Crystal structure, at 2.6-A resolution, of the Streptomyces lividans
RT   xylanase A, a member of the F family of beta-1,4-D-glycanases.";
RL   J. Biol. Chem. 269:20811-20814(1994).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 348-477, AND DISULFIDE BONDS.
RX   PubMed=11914070; DOI=10.1021/bi015865j;
RA   Notenboom V., Boraston A.B., Williams S.J., Kilburn D.G., Rose D.R.;
RT   "High-resolution crystal structures of the lectin-like xylan binding
RT   domain from Streptomyces lividans xylanase 10A with bound substrates
RT   reveal a novel mode of xylan binding.";
RL   Biochemistry 41:4246-4254(2002).
CC   -!- FUNCTION: Contributes to hydrolyze hemicellulose, the major
CC       component of plant cell-walls. XLNA and XLNB seem to act
CC       sequentially on the substrate to yield xylobiose and xylose as
CC       carbon sources.
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-xylosidic
CC       linkages in xylans.
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F)
CC       family. {ECO:0000305}.
DR   EMBL; M64551; AAC26525.1; -; Genomic_DNA.
DR   PIR; JS0589; JS0589.
DR   PDB; 1E0V; X-ray; 1.70 A; A=42-343.
DR   PDB; 1E0W; X-ray; 1.20 A; A=42-343.
DR   PDB; 1E0X; X-ray; 1.65 A; A/B=42-350.
DR   PDB; 1KNL; X-ray; 1.20 A; A=348-477.
DR   PDB; 1KNM; X-ray; 1.20 A; A=348-477.
DR   PDB; 1MC9; X-ray; 1.70 A; A=348-477.
DR   PDB; 1OD8; X-ray; 1.05 A; A=42-354.
DR   PDB; 1V0K; X-ray; 1.03 A; A=42-354.
DR   PDB; 1V0L; X-ray; 0.98 A; A=42-354.
DR   PDB; 1V0M; X-ray; 1.07 A; A=42-354.
DR   PDB; 1V0N; X-ray; 1.10 A; A=42-354.
DR   PDB; 1XAS; X-ray; 2.60 A; A=42-340.
DR   PDBsum; 1E0V; -.
DR   PDBsum; 1E0W; -.
DR   PDBsum; 1E0X; -.
DR   PDBsum; 1KNL; -.
DR   PDBsum; 1KNM; -.
DR   PDBsum; 1MC9; -.
DR   PDBsum; 1OD8; -.
DR   PDBsum; 1V0K; -.
DR   PDBsum; 1V0L; -.
DR   PDBsum; 1V0M; -.
DR   PDBsum; 1V0N; -.
DR   PDBsum; 1XAS; -.
DR   ProteinModelPortal; P26514; -.
DR   SMR; P26514; -.
DR   DrugBank; DB03389; alpha-D-Xylopyranose.
DR   DrugBank; DB04465; Lactose.
DR   CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   PRIDE; P26514; -.
DR   BRENDA; 3.2.1.8; 6052.
DR   UniPathway; UPA00114; -.
DR   EvolutionaryTrace; P26514; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
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   CDD; cd00161; RICIN; 1.
DR   InterPro; IPR001000; GH10.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF50370; SSF50370; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW   Disulfide bond; Glycosidase; Hydrolase; Lectin;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL        1     41       {ECO:0000269|PubMed:1743521}.
FT   CHAIN        42    477       Endo-1,4-beta-xylanase A.
FT                                /FTId=PRO_0000007979.
FT   DOMAIN       42    340       GH10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01096}.
FT   DOMAIN      361    477       Ricin B-type lectin.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00174}.
FT   ACT_SITE    169    169       Proton donor.
FT   ACT_SITE    277    277       Nucleophile.
FT   DISULFID    364    383       {ECO:0000255|PROSITE-ProRule:PRU00174,
FT                                ECO:0000269|PubMed:11914070}.
FT   DISULFID    406    423       {ECO:0000255|PROSITE-ProRule:PRU00174,
FT                                ECO:0000269|PubMed:11914070}.
FT   DISULFID    447    466       {ECO:0000255|PROSITE-ProRule:PRU00174,
FT                                ECO:0000269|PubMed:11914070}.
FT   HELIX        46     51       {ECO:0000244|PDB:1V0L}.
FT   TURN         52     54       {ECO:0000244|PDB:1V0L}.
FT   STRAND       56     61       {ECO:0000244|PDB:1V0L}.
FT   HELIX        63     65       {ECO:0000244|PDB:1V0L}.
FT   HELIX        69     78       {ECO:0000244|PDB:1V0L}.
FT   STRAND       80     86       {ECO:0000244|PDB:1V0L}.
FT   HELIX        90     93       {ECO:0000244|PDB:1V0L}.
FT   HELIX       103    114       {ECO:0000244|PDB:1V0L}.
FT   STRAND      118    125       {ECO:0000244|PDB:1V0L}.
FT   STRAND      127    129       {ECO:0000244|PDB:1V0L}.
FT   HELIX       132    135       {ECO:0000244|PDB:1V0L}.
FT   HELIX       139    156       {ECO:0000244|PDB:1V0L}.
FT   TURN        157    160       {ECO:0000244|PDB:1V0L}.
FT   STRAND      162    168       {ECO:0000244|PDB:1V0L}.
FT   STRAND      173    176       {ECO:0000244|PDB:1V0L}.
FT   HELIX       183    186       {ECO:0000244|PDB:1V0L}.
FT   HELIX       191    202       {ECO:0000244|PDB:1V0L}.
FT   STRAND      206    214       {ECO:0000244|PDB:1V0L}.
FT   HELIX       221    236       {ECO:0000244|PDB:1V0L}.
FT   STRAND      242    245       {ECO:0000244|PDB:1V0L}.
FT   STRAND      248    250       {ECO:0000244|PDB:1V0L}.
FT   STRAND      251    253       {ECO:0000244|PDB:1OD8}.
FT   HELIX       259    267       {ECO:0000244|PDB:1V0L}.
FT   TURN        268    270       {ECO:0000244|PDB:1V0L}.
FT   STRAND      272    280       {ECO:0000244|PDB:1V0L}.
FT   HELIX       285    296       {ECO:0000244|PDB:1V0L}.
FT   STRAND      301    307       {ECO:0000244|PDB:1V0L}.
FT   HELIX       311    313       {ECO:0000244|PDB:1V0L}.
FT   HELIX       317    319       {ECO:0000244|PDB:1V0L}.
FT   STRAND      322    324       {ECO:0000244|PDB:1V0L}.
FT   HELIX       332    341       {ECO:0000244|PDB:1V0L}.
FT   TURN        359    361       {ECO:0000244|PDB:1KNL}.
FT   STRAND      364    366       {ECO:0000244|PDB:1KNL}.
FT   HELIX       368    370       {ECO:0000244|PDB:1KNL}.
FT   STRAND      379    381       {ECO:0000244|PDB:1KNL}.
FT   HELIX       387    389       {ECO:0000244|PDB:1KNL}.
FT   STRAND      391    393       {ECO:0000244|PDB:1KNL}.
FT   STRAND      399    401       {ECO:0000244|PDB:1KNL}.
FT   TURN        402    404       {ECO:0000244|PDB:1KNL}.
FT   STRAND      405    410       {ECO:0000244|PDB:1KNL}.
FT   STRAND      417    422       {ECO:0000244|PDB:1KNL}.
FT   HELIX       427    429       {ECO:0000244|PDB:1KNL}.
FT   STRAND      431    433       {ECO:0000244|PDB:1KNL}.
FT   STRAND      439    441       {ECO:0000244|PDB:1KNL}.
FT   TURN        442    444       {ECO:0000244|PDB:1KNL}.
FT   STRAND      447    450       {ECO:0000244|PDB:1KNL}.
FT   HELIX       451    453       {ECO:0000244|PDB:1KNL}.
FT   STRAND      460    464       {ECO:0000244|PDB:1KNL}.
FT   HELIX       470    472       {ECO:0000244|PDB:1KNL}.
SQ   SEQUENCE   477 AA;  51163 MW;  E14A7FE37BDC68CC CRC64;
     MGSYALPRSG VRRSIRVLLL ALVVGVLGTA TALIAPPGAH AAESTLGAAA AQSGRYFGTA
     IASGRLSDST YTSIAGREFN MVTAENEMKI DATEPQRGQF NFSSADRVYN WAVQNGKQVR
     GHTLAWHSQQ PGWMQSLSGS ALRQAMIDHI NGVMAHYKGK IVQWDVVNEA FADGSSGARR
     DSNLQRSGND WIEVAFRTAR AADPSAKLCY NDYNVENWTW AKTQAMYNMV RDFKQRGVPI
     DCVGFQSHFN SGSPYNSNFR TTLQNFAALG VDVAITELDI QGAPASTYAN VTNDCLAVSR
     CLGITVWGVR DSDSWRSEQT PLLFNNDGSK KAAYTAVLDA LNGGDSSEPP ADGGQIKGVG
     SGRCLDVPDA STSDGTQLQL WDCHSGTNQQ WAATDAGELR VYGDKCLDAA GTSNGSKVQI
     YSCWGGDNQK WRLNSDGSVV GVQSGLCLDA VGNGTANGTL IQLYTCSNGS NQRWTRT
//
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