XYNA_FUSO4
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 25-MAY-2022, entry version 47.
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}.
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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 UniPathway; UPA00114; -.
DR Proteomes; UP000009097; Unplaced.
DR GO; GO:0005615; C:extracellular space; 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 InterPro; IPR044846; GH10.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490; PTHR31490; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; SSF51445; 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 Reference proteome; 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
