XYNA_EMENI
ID XYNA_EMENI Reviewed; 225 AA.
AC P55332; C8V464; Q00173; Q1HFT4; Q5B767;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 124.
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 AltName: Full=22 kDa xylanase;
DE AltName: Full=Xylanase X22;
DE Flags: Precursor;
GN Name=xlnA; ORFNames=AN3613;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8787417; DOI=10.1128/aem.62.6.2179-2182.1996;
RA Perez-Gonzalez J.A., de Graaff L.H., Visser J., Ramon D.;
RT "Molecular cloning and expression in Saccharomyces cerevisiae of two
RT Aspergillus nidulans xylanase genes.";
RL Appl. Environ. Microbiol. 62:2179-2182(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16844780; DOI=10.1073/pnas.0604632103;
RA Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.;
RT "Development and application of a suite of polysaccharide-degrading enzymes
RT for analyzing plant cell walls.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [5]
RP INDUCTION.
RX PubMed=9495775; DOI=10.1128/jb.180.5.1331-1333.1998;
RA MacCabe A.P., Orejas M., Perez-Gonzalez J.A., Ramon D.;
RT "Opposite patterns of expression of two Aspergillus nidulans xylanase genes
RT with respect to ambient pH.";
RL J. Bacteriol. 180:1331-1333(1998).
RN [6]
RP BIOTECHNOLOGY.
RX PubMed=10359487; DOI=10.1016/s0168-1605(98)00202-5;
RA Ganga M.A., Pinaga F., Valles S., Ramon D., Querol A.;
RT "Aroma improving in microvinification processes by the use of a recombinant
RT wine yeast strain expressing the Aspergillus nidulans xlnA gene.";
RL Int. J. Food Microbiol. 47:171-178(1999).
RN [7]
RP INDUCTION.
RX PubMed=9987120; DOI=10.1046/j.1365-2958.1999.01157.x;
RA Orejas M., MacCabe A.P., Perez Gonzalez J.A., Kumar S., Ramon D.;
RT "Carbon catabolite repression of the Aspergillus nidulans xlnA gene.";
RL Mol. Microbiol. 31:177-184(1999).
RN [8]
RP INDUCTION.
RX PubMed=18420433; DOI=10.1016/j.fgb.2008.03.002;
RA Tamayo E.N., Villanueva A., Hasper A.A., de Graaff L.H., Ramon D.,
RA Orejas M.;
RT "CreA mediates repression of the regulatory gene xlnR which controls the
RT production of xylanolytic enzymes in Aspergillus nidulans.";
RL Fungal Genet. Biol. 45:984-993(2008).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=25043916; DOI=10.1186/1471-2164-15-613;
RA Martins I., Hartmann D.O., Alves P.C., Martins C., Garcia H.,
RA Leclercq C.C., Ferreira R., He J., Renaut J., Becker J.D.,
RA Silva Pereira C.;
RT "Elucidating how the saprophytic fungus Aspergillus nidulans uses the plant
RT polyester suberin as carbon source.";
RL BMC Genomics 15:613-613(2014).
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:16844780,
CC ECO:0000269|PubMed:8787417}.
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 5.4. {ECO:0000269|PubMed:16844780};
CC Temperature dependence:
CC Optimum temperature is 52 degrees Celsius.
CC {ECO:0000269|PubMed:16844780};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25043916,
CC ECO:0000269|PubMed:8787417}.
CC -!- INDUCTION: Expressed in the presence of D-xylose under conditions of
CC alkaline ambient pH, probably under the regulation of the pacC
CC transcription factor. Repressed in presence of glucose through the
CC action of the creA transcription repressor.
CC {ECO:0000269|PubMed:18420433, ECO:0000269|PubMed:9495775,
CC ECO:0000269|PubMed:9987120}.
CC -!- BIOTECHNOLOGY: An increase in fruity aroma was organoleptically
CC detected in the wine produced by the recombinant wine yeast strain T73
CC expressing xnlA. {ECO:0000269|PubMed:10359487}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000305}.
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DR EMBL; Z49892; CAA90073.1; -; Genomic_DNA.
DR EMBL; DQ490490; ABF50866.1; -; mRNA.
DR EMBL; AACD01000061; EAA59821.1; -; Genomic_DNA.
DR EMBL; BN001302; CBF75776.1; -; Genomic_DNA.
DR PIR; S57477; S57477.
DR RefSeq; XP_661217.1; XM_656125.1.
DR AlphaFoldDB; P55332; -.
DR SMR; P55332; -.
DR STRING; 162425.CADANIAP00005129; -.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR CLAE; XYN11A_EMENI; -.
DR EnsemblFungi; CBF75776; CBF75776; ANIA_03613.
DR EnsemblFungi; EAA59821; EAA59821; AN3613.2.
DR GeneID; 2873037; -.
DR KEGG; ani:AN3613.2; -.
DR VEuPathDB; FungiDB:AN3613; -.
DR eggNOG; ENOG502RXA7; Eukaryota.
DR HOGENOM; CLU_052631_0_0_1; -.
DR InParanoid; P55332; -.
DR OMA; NMQNHFN; -.
DR OrthoDB; 1306131at2759; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; 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; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW Xylan degradation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..225
FT /note="Endo-1,4-beta-xylanase A"
FT /id="PRO_0000008004"
FT DOMAIN 37..225
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT ACT_SITE 121
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT ACT_SITE 212
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
SQ SEQUENCE 225 AA; 24070 MW; 670F2C79602C7FEC CRC64;
MVSFKSLLVL CCAALGAFAT PVGSEDLAAR EASLLERSTP SSTGWSNGYY YSFWTDGGGD
VTYTNGAGGS YTVQWSNVGN FVGGKGWNPG STRTINYGGS FNPSGNGYLA VYGWTQNPLI
EYYIVESYGT YNPGSGGQHR GTVYSDGATY DIYTATRYNA PSIEGTATFE QFWSVRQSKR
TGGTVTTANH FNAWAALGMR LGTHNYQIVA TEGYQSSGSA SITVY
