XYNA_ASPFU
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 25-MAY-2022, entry version 101.
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;
OC Aspergillus subgen. Fumigati.
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 Aspergillus
RT 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 fumigatus
RT 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., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., 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., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA 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 xylan, a
CC major structural heterogeneous polysaccharide found in plant biomass
CC representing the second most abundant polysaccharide in the biosphere,
CC after cellulose. {ECO:0000269|PubMed:19577187}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC 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 activity
CC is retained at 70 degrees Celsius. Stable from 30 to 60 degrees
CC 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) family.
CC {ECO:0000305}.
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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 AlphaFoldDB; Q4WG11; -.
DR SMR; Q4WG11; -.
DR STRING; 746128.CADAFUBP00004715; -.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR CLAE; XYN11A_ASPFU; -.
DR EnsemblFungi; EAL86316; EAL86316; AFUA_3G00320.
DR GeneID; 3505821; -.
DR KEGG; afm:AFUA_3G00320; -.
DR VEuPathDB; FungiDB:Afu3g00320; -.
DR eggNOG; ENOG502RXA7; Eukaryota.
DR HOGENOM; CLU_052631_0_0_1; -.
DR InParanoid; Q4WG11; -.
DR OMA; NMQNHFN; -.
DR OrthoDB; 1306131at2759; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000002530; Chromosome 3.
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; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW Xylan degradation.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..228
FT /note="Endo-1,4-beta-xylanase xynf11a"
FT /id="PRO_0000393161"
FT DOMAIN 40..228
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT ACT_SITE 124
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT ACT_SITE 215
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="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
