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Database: UniProt
Entry: Q4WG11
LinkDB: Q4WG11
Original site: Q4WG11 
ID   XYNA_ASPFU              Reviewed;         228 AA.
AC   Q4WG11;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   10-APR-2019, entry version 90.
DE   RecName: Full=Endo-1,4-beta-xylanase xynf11a;
DE            Short=Xylanase xynf11a;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase xynf11a;
DE   Flags: Precursor;
GN   Name=xlnA; Synonyms=xynf11a; ORFNames=AFUA_3G00320;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=SL1;
RA   Dabrowski S., Ahring B.K.;
RT   "Characterization of recombinant xylan degrading enzymes from
RT   Aspergillus fumigatus isolate SL1.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=MKU1;
RX   PubMed=19577187; DOI=10.1016/j.jbiosc.2009.02.003;
RA   Jeya M., Thiagarajan S., Lee J.K., Gunasekaran P.;
RT   "Cloning and expression of GH11 xylanase gene from Aspergillus
RT   fumigatus MKU1 in Pichia pastoris.";
RL   J. Biosci. Bioeng. 108:24-29(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S.,
RA   Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W.,
RA   Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S.,
RA   Farman M.L., Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R.,
RA   Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A.,
RA   Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J.,
RA   Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J.,
RA   Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S.,
RA   Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A.,
RA   Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M.,
RA   Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I.,
RA   Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M.,
RA   Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S.,
RA   Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J.,
RA   White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K.,
RA   Machida M., Hall N., Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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:0000269|PubMed:19577187}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in
CC         xylans.; EC=3.2.1.8;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0. Stable in the pH range from 4.0 to 8.0.
CC         {ECO:0000269|PubMed:19577187};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius. Around 53 percent
CC         activity is retained at 70 degrees Celsius. Stable from 30 to 60
CC         degrees Celsius with maximum stability at 30 degrees Celsius.
CC         {ECO:0000269|PubMed:19577187};
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; DQ156553; ABA40419.1; -; mRNA.
DR   EMBL; EF375873; ABN48478.1; -; Genomic_DNA.
DR   EMBL; AAHF01000010; EAL86316.1; -; Genomic_DNA.
DR   RefSeq; XP_748354.1; XM_743261.1.
DR   ProteinModelPortal; Q4WG11; -.
DR   SMR; Q4WG11; -.
DR   STRING; 746128.CADAFUBP00004715; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   mycoCLAP; XYN11A_ASPFU; -.
DR   EnsemblFungi; EAL86316; EAL86316; AFUA_3G00320.
DR   GeneID; 3505821; -.
DR   KEGG; afm:AFUA_3G00320; -.
DR   EuPathDB; FungiDB:Afu3g00320; -.
DR   HOGENOM; HOG000179135; -.
DR   InParanoid; Q4WG11; -.
DR   KO; K01181; -.
DR   OMA; NMQNHFN; -.
DR   OrthoDB; 1306131at2759; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000002530; Chromosome 3.
DR   Proteomes; UP000002530; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IDA:UniProtKB.
DR   GO; GO:0045493; P:xylan catabolic process; IDA: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   1: Evidence at protein level;
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    228       Endo-1,4-beta-xylanase xynf11a.
FT                                /FTId=PRO_0000393161.
FT   DOMAIN       40    228       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    124    124       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    215    215       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10063}.
FT   CARBOHYD     29     29       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
SQ   SEQUENCE   228 AA;  24494 MW;  7DBED47138DA238F CRC64;
     MVSFSYLLLA CSAIGALAAP VEPETTSFNE TALHEFAERA GTPSSTGWNN GYYYSFWTDG
     GGDVTYTNGA GGSYSVNWRN VGNFVGGKGW NPGSARTINY GGSFNPSGNG YLAVYGWTTN
     PLIEYYVVES YGTYNPGSGG TFRGTVNTDG GTYNIYTAVR YNAPSIEGTK TFTQYWSVRT
     SKRTGGTVTM ANHFNAWSRL GMNLGTHNYQ IVATEGYQSS GSASITVY
//
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