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Database: UniProt
Entry: A1CCU0
LinkDB: A1CCU0
Original site: A1CCU0 
ID   XYNA_ASPCL              Reviewed;         229 AA.
AC   A1CCU0;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   16-JAN-2019, entry version 63.
DE   RecName: Full=Probable 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; ORFNames=ACLA_063140;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC
OS   3887 / NRRL 1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P.,
RA   Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A.,
RA   Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A.,
RA   Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R.,
RA   Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M.,
RA   Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R.,
RA   Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R.,
RA   Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of
CC       xylan, a major structural heterogeneous polysaccharide found in
CC       plant biomass representing the second most abundant polysaccharide
CC       in the biosphere, after cellulose. {ECO:0000250}.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000305}.
DR   EMBL; DS027050; EAW12347.1; -; Genomic_DNA.
DR   RefSeq; XP_001273773.1; XM_001273772.1.
DR   ProteinModelPortal; A1CCU0; -.
DR   SMR; A1CCU0; -.
DR   STRING; 5057.CADACLAP00005741; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   PRIDE; A1CCU0; -.
DR   EnsemblFungi; EAW12347; EAW12347; ACLA_063140.
DR   GeneID; 4706056; -.
DR   KEGG; act:ACLA_063140; -.
DR   EuPathDB; FungiDB:ACLA_063140; -.
DR   HOGENOM; HOG000179135; -.
DR   KO; K01181; -.
DR   OMA; GAFSAQW; -.
DR   OrthoDB; 1306131at2759; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; ISS:UniProtKB.
DR   GO; GO:0045493; P:xylan catabolic process; ISS:UniProtKB.
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   3: Inferred from homology;
KW   Carbohydrate metabolism; Complete proteome; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW   Signal; Xylan degradation.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19    229       Probable endo-1,4-beta-xylanase A.
FT                                /FTId=PRO_0000393158.
FT   DOMAIN       41    229       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    125    125       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    216    216       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10063}.
FT   CARBOHYD     30     30       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    100    100       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
SQ   SEQUENCE   229 AA;  25004 MW;  E46E193D612C9281 CRC64;
     MVSFKYLFLA ASALGALAAP VEVEESSWFN ETALHEFAER AGTPSSTGWN NGYYYSFWTD
     NGGTVNYQNG NGGSYSVQWK DTGNFVGGKG WNPGSARTIN YSGSFNPSGN AYLTVYGWTT
     NPLVEYYIVE NYGTYNPGNG GTYRGSVYSD GANYNIYTAT RYNAPSIEGD KTFTQYWSVR
     QSKRTGGTVT TANHFNAWAQ LGMSLGTHNY QIVATEGYQS SGSSSITVY
//
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