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Database: UniProt
Entry: P55333
LinkDB: P55333
Original site: P55333 
ID   XYNB_EMENI              Reviewed;         221 AA.
AC   P55333; C8VR70; Q00176; Q5AQR5;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   16-JAN-2019, entry version 115.
DE   RecName: Full=Endo-1,4-beta-xylanase B;
DE            Short=Xylanase B;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase B;
DE   AltName: Full=24 kDa xylanase;
DE   AltName: Full=Endo-1,4-beta-xylanase G1;
DE            Short=Xylanase G1;
DE   AltName: Full=Xylanase X24;
DE   Flags: Precursor;
GN   Name=xlnB; Synonyms=xynB, xynG1; ORFNames=AN9365;
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 [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   [3]
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   [4]
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   [5]
RP   INDUCTION.
RX   PubMed=11160081; DOI=10.1128/JB.183.5.1517-1523.2001;
RA   Orejas M., MacCabe A.P., Perez-Gonzalez J.A., Kumar S., Ramon D.;
RT   "The wide-domain carbon catabolite repressor CreA indirectly controls
RT   expression of the Aspergillus nidulans xlnB gene, encoding the acidic
RT   endo-beta-(1,4)-xylanase X(24).";
RL   J. Bacteriol. 183:1517-1523(2001).
RN   [6]
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:8787417}.
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:0000269|PubMed:8787417}.
CC   -!- INDUCTION: Expressed in the presence of D-xylose under conditions
CC       of acidic 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:11160081, ECO:0000269|PubMed:18420433,
CC       ECO:0000269|PubMed:9495775}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000305}.
DR   EMBL; Z49893; CAA90074.1; -; Genomic_DNA.
DR   EMBL; AACD01000172; EAA66432.1; -; Genomic_DNA.
DR   EMBL; BN001308; CBF87481.1; -; Genomic_DNA.
DR   PIR; S57469; S57469.
DR   RefSeq; XP_682634.1; XM_677542.1.
DR   ProteinModelPortal; P55333; -.
DR   SMR; P55333; -.
DR   STRING; 162425.CADANIAP00001152; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   EnsemblFungi; CBF87481; CBF87481; ANIA_09365.
DR   EnsemblFungi; EAA66432; EAA66432; AN9365.2.
DR   GeneID; 2867930; -.
DR   KEGG; ani:AN9365.2; -.
DR   HOGENOM; HOG000179135; -.
DR   InParanoid; P55333; -.
DR   KO; K01181; -.
DR   OMA; IEYYVVD; -.
DR   OrthoDB; 1306131at2759; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000000560; Chromosome VIII.
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; IBA:GO_Central.
DR   GO; GO:0045493; P:xylan catabolic process; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Complete proteome; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19    221       Endo-1,4-beta-xylanase B.
FT                                /FTId=PRO_0000008005.
FT   DOMAIN       33    221       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    117    117       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    208    208       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10063}.
FT   CONFLICT     73     73       N -> K (in Ref. 1; CAA90074).
FT                                {ECO:0000305}.
FT   CONFLICT     98     98       N -> I (in Ref. 1; CAA90074).
FT                                {ECO:0000305}.
SQ   SEQUENCE   221 AA;  23504 MW;  B762F0BB4B3F77C3 CRC64;
     MVSFSSLLLA CSAVTAFAAP SDQSIAERSL SERSTPSSTG TSGGYYYSFW TDGGGDVTYT
     NGDGGSYTVE WTNVGNFVGG KGWNPGSSQT ISYSGSFNPS GNGYLSVYGW TQNPLIEYYI
     VESYGDYNPG TAGTHQGTLE SDGSTYDIYT ATRENAPSIE GTATFTQFWS VRQSKRTSGS
     VTTQNHFDAW SQLGMTLGTH NYQIVAVEGY QSSGSASITV S
//
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