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Database: UniProt
Entry: P55332
LinkDB: P55332
Original site: P55332 
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   16-JAN-2019, entry version 111.
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
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=8787417;
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
RP   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
RT   enzymes 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.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   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.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [5]
RP   INDUCTION.
RX   PubMed=9495775;
RA   MacCabe A.P., Orejas M., Perez-Gonzalez J.A., Ramon D.;
RT   "Opposite patterns of expression of two Aspergillus nidulans xylanase
RT   genes 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
RT   recombinant wine yeast strain expressing the Aspergillus nidulans xlnA
RT   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
RT   the production of xylanolytic enzymes in Aspergillus nidulans.";
RL   Fungal Genet. Biol. 45:984-993(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:0000269|PubMed:16844780,
CC       ECO:0000269|PubMed:8787417}.
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 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:8787417}.
CC   -!- INDUCTION: Expressed in the presence of D-xylose under conditions
CC       of 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
CC       T73 expressing xnlA. {ECO:0000269|PubMed:10359487}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000305}.
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   ProteinModelPortal; P55332; -.
DR   SMR; P55332; -.
DR   STRING; 162425.CADANIAP00005129; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   mycoCLAP; XYN11A_EMENI; -.
DR   PRIDE; P55332; -.
DR   EnsemblFungi; CBF75776; CBF75776; ANIA_03613.
DR   EnsemblFungi; EAA59821; EAA59821; AN3613.2.
DR   GeneID; 2873037; -.
DR   KEGG; ani:AN3613.2; -.
DR   HOGENOM; HOG000179135; -.
DR   InParanoid; P55332; -.
DR   KO; K01181; -.
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; Complete proteome; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    225       Endo-1,4-beta-xylanase A.
FT                                /FTId=PRO_0000008004.
FT   DOMAIN       37    225       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    121    121       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    212    212       Proton donor. {ECO:0000255|PROSITE-
FT                                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
//
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