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 24-JAN-2024, entry version 132.
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 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 [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 [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., 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 [4]
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 [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 endo-
RT 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 the
RT 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 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:8787417}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC 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 of
CC 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) family.
CC {ECO:0000305}.
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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 AlphaFoldDB; P55333; -.
DR SMR; P55333; -.
DR STRING; 227321.P55333; -.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR EnsemblFungi; CBF87481; CBF87481; ANIA_09365.
DR GeneID; 2867930; -.
DR KEGG; ani:AN9365.2; -.
DR eggNOG; ENOG502RXA7; Eukaryota.
DR HOGENOM; CLU_052631_0_0_1; -.
DR InParanoid; P55333; -.
DR OMA; VDWTNCG; -.
DR OrthoDB; 1778490at2759; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
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 PANTHER; PTHR46828; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR PANTHER; PTHR46828:SF2; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR Pfam; PF00457; Glyco_hydro_11; 1.
DR PRINTS; PR00911; GLHYDRLASE11.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW Xylan degradation.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..221
FT /note="Endo-1,4-beta-xylanase B"
FT /id="PRO_0000008005"
FT DOMAIN 33..221
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT ACT_SITE 117
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT ACT_SITE 208
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT CONFLICT 73
FT /note="N -> K (in Ref. 1; CAA90074)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="N -> I (in Ref. 1; CAA90074)"
FT /evidence="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
//
