ID   XYNA_FUSO4              Reviewed;         327 AA.
AC   B3A0S5; J9NQE2;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
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=Endo-1,4-beta-xylanase GH10 A;
DE            Short=FoXyn10a;
DE   AltName: Full=Xylanase III;
GN   ORFNames=FOXG_17421;
OS   Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935
OS   / NRRL 34936) (Fusarium vascular wilt of tomato).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=426428;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 25-327.
RC   STRAIN=4287 / CBS 123668 / FGSC 9935 / NRRL 34936;
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA   Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA   Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA   Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA   Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
RN   [2]
RP   PROTEIN SEQUENCE OF 168-182 AND 290-313, FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=F3;
RX   PubMed=9291571; DOI=10.1016/s0008-6215(97)00075-x;
RA   Christakopoulos P., Nerinckx W., Kekos D., Macris B., Claeyssens M.;
RT   "The alkaline xylanase III from Fusarium oxysporum F3 belongs to family
RT   F/10.";
RL   Carbohydr. Res. 302:191-195(1997).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS), PROTEIN SEQUENCE OF 1-24,
RP   GLYCOSYLATION AT ASN-101, ACTIVE SITES, AND DISULFIDE BONDS.
RC   STRAIN=F3;
RX   PubMed=22751658; DOI=10.1107/s0907444912007044;
RA   Dimarogona M., Topakas E., Christakopoulos P., Chrysina E.D.;
RT   "The structure of a GH10 xylanase from Fusarium oxysporum reveals the
RT   presence of an extended loop on top of the catalytic cleft.";
RL   Acta Crystallogr. 68:735-742(2012).
CC   -!- FUNCTION: Catalyzes the hydrolysis of the internal glycosidic bonds in
CC       heteroxylans, releasing mainly xylobiose and xylotriose. Most active on
CC       oat-spelt xylan. {ECO:0000269|PubMed:9291571}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8; Evidence={ECO:0000269|PubMed:9291571};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=1.22 mmol/min/mg enzyme {ECO:0000269|PubMed:9291571};
CC       pH dependence:
CC         Optimum pH is 6-8. {ECO:0000269|PubMed:9291571};
CC       Temperature dependence:
CC         Optimum temperature is 40-50 degrees Celsius.
CC         {ECO:0000269|PubMed:9291571};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9291571}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000269|PubMed:9291571}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAXH01001232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PDB; 3U7B; X-ray; 1.94 A; A/B/C/D/E=1-327.
DR   PDBsum; 3U7B; -.
DR   AlphaFoldDB; B3A0S5; -.
DR   SMR; B3A0S5; -.
DR   STRING; 426428.B3A0S5; -.
DR   iPTMnet; B3A0S5; -.
DR   OrthoDB; 548101at2759; -.
DR   UniPathway; UPA00114; -.
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; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490:SF35; ENDO-1,4-BETA-XYLANASE; 1.
DR   PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Hydrolase; Polysaccharide degradation;
KW   Secreted; Xylan degradation.
FT   CHAIN           1..327
FT                   /note="Endo-1,4-beta-xylanase A"
FT                   /id="PRO_0000415231"
FT   DOMAIN          1..323
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        131
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000269|PubMed:22751658"
FT   ACT_SITE        245
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10061,
FT                   ECO:0000269|PubMed:22751658"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:22751658"
FT   DISULFID        81..123
FT                   /evidence="ECO:0000269|PubMed:22751658"
FT   DISULFID        273..279
FT                   /evidence="ECO:0000269|PubMed:22751658"
FT   HELIX           5..11
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   STRAND          16..21
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   HELIX           28..33
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   TURN            36..38
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   STRAND          41..46
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   HELIX           50..53
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   HELIX           63..73
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   TURN            74..76
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   STRAND          78..87
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   HELIX           92..95
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   HELIX           101..118
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   TURN            119..122
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   STRAND          124..130
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   STRAND          137..139
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   HELIX           143..148
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   HELIX           152..163
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   STRAND          167..175
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   HELIX           181..195
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   STRAND          202..205
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   STRAND          208..212
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   HELIX           224..235
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   TURN            236..238
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   STRAND          240..253
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   HELIX           256..275
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   STRAND          279..285
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   HELIX           289..291
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   HELIX           294..297
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   STRAND          305..307
FT                   /evidence="ECO:0007829|PDB:3U7B"
FT   HELIX           315..325
FT                   /evidence="ECO:0007829|PDB:3U7B"
SQ   SEQUENCE   327 AA;  36198 MW;  DC4D2D291A37E7A0 CRC64;
     AASGLEAAMK AAGKQYFGTA LTVRNDQGEI DIINNKNEIG SITPENAMKW EAIQPNRGQF
     NWGPADQHAA AATSRGYELR CHTLVWHSQL PSWVANGNWN NQTLQAVMRD HINAVMGRYR
     GKCTHWDVVN EALNEDGTYR DSVFLRVIGE AYIPIAFRMA LAADPTTKLY YNDYNLEYGN
     AKTEGAKRIA RLVKSYGLRI DGIGLQAHMT SESTPTQNTP TPSRAKLASV LQGLADLGVD
     VAYTELDIRM NTPATQQKLQ TNADAYARIV GSCMDVKRCV GITVWGISDK YSWVPGTFPG
     EGSALLWNDN FQKKPSYTST LNTINRR
//