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Database: UniProt
Entry: P33557
LinkDB: P33557
Original site: P33557 
ID   XYN3_ASPKW              Reviewed;         211 AA.
AC   P33557; G7XQI2;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 2.
DT   10-APR-2019, entry version 111.
DE   RecName: Full=Endo-1,4-beta-xylanase 3;
DE            Short=Xylanase 3;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase 3;
DE   AltName: Full=Xylanase C;
DE   Flags: Precursor;
GN   Name=xynC; ORFNames=AKAW_07136;
OS   Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS   awamori var. kawachi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1033177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 28-34.
RC   STRAIN=NBRC 4308;
RX   PubMed=1368843; DOI=10.1271/bbb.56.1338;
RA   Ito K., Iwashita K., Iwano K.;
RT   "Cloning and sequencing of the xynC gene encoding acid xylanase of
RT   Aspergillus kawachii.";
RL   Biosci. Biotechnol. Biochem. 56:1338-1340(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 4308;
RX   PubMed=22045919; DOI=10.1128/EC.05224-11;
RA   Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y.,
RA   Takashita H., Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT   "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308,
RT   used for brewing the Japanese distilled spirit shochu.";
RL   Eukaryot. Cell 10:1586-1587(2011).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 29-210.
RC   STRAIN=NBRC 4308;
RX   PubMed=9930661; DOI=10.1093/protein/11.12.1121;
RA   Fushinobu S., Ito K., Konno M., Wakagi T., Matsuzawa H.;
RT   "Crystallographic and mutational analyses of an extremely acidophilic
RT   and acid-stable xylanase: biased distribution of acidic residues and
RT   importance of Asp-37 for catalysis at low pH.";
RL   Protein Eng. 11:1121-1128(1998).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in
CC         xylans.; EC=3.2.1.8;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000305}.
DR   EMBL; S45138; AAC60542.1; -; Genomic_DNA.
DR   EMBL; D14848; BAA03576.1; -; Genomic_DNA.
DR   EMBL; DF126466; GAA89022.1; -; Genomic_DNA.
DR   PDB; 1BK1; X-ray; 2.00 A; A=28-211.
DR   PDB; 3RI8; X-ray; 2.00 A; A=28-211.
DR   PDB; 3RI9; X-ray; 2.00 A; A=28-211.
DR   PDBsum; 1BK1; -.
DR   PDBsum; 3RI8; -.
DR   PDBsum; 3RI9; -.
DR   ProteinModelPortal; P33557; -.
DR   SMR; P33557; -.
DR   STRING; 40384.P33557; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   InParanoid; P33557; -.
DR   UniPathway; UPA00114; -.
DR   EvolutionaryTrace; P33557; -.
DR   Proteomes; UP000006812; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL        1     27       {ECO:0000269|PubMed:1368843}.
FT   CHAIN        28    211       Endo-1,4-beta-xylanase 3.
FT                                /FTId=PRO_0000007991.
FT   DOMAIN       28    210       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    106    106       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    197    197       Proton donor.
FT   DISULFID    119    138
FT   CONFLICT      7      7       F -> S (in Ref. 1; AAC60542/BAA03576).
FT                                {ECO:0000305}.
FT   CONFLICT     12     13       VT -> GH (in Ref. 1; AAC60542/BAA03576).
FT                                {ECO:0000305}.
FT   CONFLICT     21     21       E -> Q (in Ref. 1; AAC60542/BAA03576).
FT                                {ECO:0000305}.
FT   CONFLICT     42     42       G -> A (in Ref. 1; AAC60542/BAA03576).
FT                                {ECO:0000305}.
FT   CONFLICT     80     80       T -> S (in Ref. 1; AAC60542/BAA03576).
FT                                {ECO:0000305}.
FT   STRAND       33     38       {ECO:0000244|PDB:1BK1}.
FT   HELIX        39     41       {ECO:0000244|PDB:1BK1}.
FT   STRAND       42     47       {ECO:0000244|PDB:1BK1}.
FT   HELIX        48     50       {ECO:0000244|PDB:1BK1}.
FT   STRAND       52     63       {ECO:0000244|PDB:1BK1}.
FT   STRAND       65     73       {ECO:0000244|PDB:1BK1}.
FT   STRAND       79     86       {ECO:0000244|PDB:1BK1}.
FT   STRAND       90    100       {ECO:0000244|PDB:1BK1}.
FT   TURN        101    104       {ECO:0000244|PDB:1BK1}.
FT   STRAND      105    115       {ECO:0000244|PDB:1BK1}.
FT   TURN        118    121       {ECO:0000244|PDB:1BK1}.
FT   STRAND      122    130       {ECO:0000244|PDB:1BK1}.
FT   STRAND      133    147       {ECO:0000244|PDB:1BK1}.
FT   STRAND      150    163       {ECO:0000244|PDB:1BK1}.
FT   STRAND      166    170       {ECO:0000244|PDB:1BK1}.
FT   HELIX       172    179       {ECO:0000244|PDB:1BK1}.
FT   HELIX       180    182       {ECO:0000244|PDB:1BK1}.
FT   STRAND      187    210       {ECO:0000244|PDB:1BK1}.
SQ   SEQUENCE   211 AA;  22627 MW;  86EFBEE12A869022 CRC64;
     MKVTAAFAGL LVTAFAAPVP EPVLVSRSAG INYVQNYNGN LGDFTYDESA GTFSMYWEDG
     VSSDFVVGLG WTTGSSNAIT YSAEYSASGS SSYLAVYGWV NYPQAEYYIV EDYGDYNPCS
     SATSLGTVYS DGSTYQVCTD TRTNEPSITG TSTFTQYFSV RESTRTSGTV TVANHFNFWA
     QHGFGNSDFN YQVMAVEAWS GAGSASVTIS S
//
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