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 27-MAR-2024, entry version 93.
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}.
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DR EMBL; CM003148; KIS68312.1; -; Genomic_DNA.
DR RefSeq; XP_011389883.1; XM_011391581.1.
DR AlphaFoldDB; Q4P902; -.
DR SMR; Q4P902; -.
DR STRING; 237631.Q4P902; -.
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; ITTVMKQ; -.
DR OrthoDB; 754421at2759; -.
DR UniPathway; UPA00114; -.
DR PHI-base; PHI:12059; -.
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 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:SF76; ENDO-1,4-BETA-XYLANASE C; 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 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
//
