ID   XIN1_USTMA              Reviewed;         344 AA.
AC   Q4P902; A0A0D1C3K5;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Endo-1,4-beta-xylanase UM03411;
DE            Short=Xylanase UM03411;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase UM03411;
DE   Flags: Precursor;
GN   ORFNames=UMAG_03411;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   INDUCTION.
RX   PubMed=10882531; DOI=10.1006/fgbi.2000.1196;
RA   Cano-Canchola C., Acevedo L., Ponce-Noyola P., Flores-Martinez A.,
RA   Flores-Carreon A., Leal-Morales C.A.;
RT   "Induction of lytic enzymes by the interaction of Ustilago maydis with Zea
RT   mays tissues.";
RL   Fungal Genet. Biol. 29:145-151(2000).
RN   [4]
RP   INDUCTION.
RX   PubMed=21062173; DOI=10.1094/phyto-01-10-0011;
RA   Nadal M., Garcia-Pedrajas M.D., Gold S.E.;
RT   "The snf1 gene of Ustilago maydis acts as a dual regulator of cell wall
RT   degrading enzymes.";
RL   Phytopathology 100:1364-1372(2010).
RN   [5]
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=22300648; DOI=10.1186/1471-2164-13-57;
RA   Couturier M., Navarro D., Olive C., Chevret D., Haon M., Favel A.,
RA   Lesage-Meessen L., Henrissat B., Coutinho P.M., Berrin J.G.;
RT   "Post-genomic analyses of fungal lignocellulosic biomass degradation reveal
RT   the unexpected potential of the plant pathogen Ustilago maydis.";
RL   BMC Genomics 13:57-57(2012).
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.
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:22300648}.
CC   -!- INDUCTION: Induced in presence of Zea mays leaves and by xylan, and
CC       repressed by glucose. SNF1 acts as a positive regulator through the
CC       release of glucose repression. {ECO:0000269|PubMed:10882531,
CC       ECO:0000269|PubMed:21062173}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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; CM003148; KIS68312.1; -; Genomic_DNA.
DR   RefSeq; XP_011389883.1; XM_011391581.1.
DR   AlphaFoldDB; Q4P902; -.
DR   SMR; Q4P902; -.
DR   STRING; 5270.UM03411P0; -.
DR   EnsemblFungi; KIS68312; KIS68312; UMAG_03411.
DR   GeneID; 23563870; -.
DR   KEGG; uma:UMAG_03411; -.
DR   VEuPathDB; FungiDB:UMAG_03411; -.
DR   eggNOG; ENOG502QSCW; Eukaryota.
DR   HOGENOM; CLU_020161_5_0_1; -.
DR   InParanoid; Q4P902; -.
DR   OMA; PENQMKW; -.
DR   OrthoDB; 829814at2759; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000000561; Chromosome 9.
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   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   Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW   Signal; Xylan degradation.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..344
FT                   /note="Endo-1,4-beta-xylanase UM03411"
FT                   /id="PRO_0000429749"
FT   DOMAIN          35..338
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        166
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        275
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        310
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        323
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        293..299
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   344 AA;  37592 MW;  84DF4BB41F30630C CRC64;
     MKTNFLVLLS ALLAASSAVT ATLIPAKCKH EAFSQRAGSS LNAAIKSDGR KYFGTCADPG
     TLGNWQISNI IKAEMGQVTP ENSMKWDATQ PQRGTFNFGN ADRLVDFATS NGKLIRGHTL
     VWHSQLPSWV SSITDANDLT NVIQNRIATV VGRYKGKVYA WDVVNEMFNE NGSFRESVFY
     KLLGEDFVKI AFEAARKADP NAKLYINDYN LDDPDYPKLK SLVANVKKWR SQGVPIDGIG
     SQSHLQAAGH FLDASKVGGA MQALCAAASE CAMTELDIAQ ASPDQYTKAT EACLNQKNCV
     GITVWGVSDN TSWRKNANPL LWNSSYQKKP AYNAVLSTLN SYQA