XY11A_USTMA
ID XY11A_USTMA Reviewed; 221 AA.
AC Q4P0L3; A0A0D1E285;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Endo-1,4-beta-xylanase 11A;
DE Short=Xylanase 11A;
DE EC=3.2.1.8;
DE AltName: Full=1,4-beta-D-xylan xylanohydrolase 11A;
DE Flags: Precursor;
GN Name=XYN11A; ORFNames=UMAG_06350;
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).
RN [6]
RP SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23889751; DOI=10.1186/1472-6750-13-59;
RA Geiser E., Wierckx N., Zimmermann M., Blank L.M.;
RT "Identification of an endo-1,4-beta-xylanase of Ustilago maydis.";
RL BMC Biotechnol. 13:59-59(2013).
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:23889751}.
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:23889751};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22300648,
CC ECO:0000269|PubMed:23889751}.
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 -!- DISRUPTION PHENOTYPE: Reduces the rate of xylan degradation and growth
CC on minimal medium with xylan. {ECO:0000269|PubMed:23889751}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000305}.
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DR EMBL; CM003143; KIS70264.1; -; Genomic_DNA.
DR RefSeq; XP_011388331.1; XM_011390029.1.
DR AlphaFoldDB; Q4P0L3; -.
DR SMR; Q4P0L3; -.
DR STRING; 5270.UM06350P0; -.
DR EnsemblFungi; KIS70264; KIS70264; UMAG_06350.
DR GeneID; 23565964; -.
DR KEGG; uma:UMAG_06350; -.
DR VEuPathDB; FungiDB:UMAG_06350; -.
DR eggNOG; ENOG502RXA7; Eukaryota.
DR HOGENOM; CLU_052631_3_2_1; -.
DR InParanoid; Q4P0L3; -.
DR OMA; NWNTQDD; -.
DR OrthoDB; 1306131at2759; -.
DR BRENDA; 3.2.1.8; 6587.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000000561; Chromosome 4.
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; IPR033123; GH11_dom.
DR InterPro; IPR001137; Glyco_hydro_11.
DR Pfam; PF00457; Glyco_hydro_11; 1.
DR PRINTS; PR00911; GLHYDRLASE11.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS00776; GH11_1; 1.
DR PROSITE; PS51761; GH11_3; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycoprotein; 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 11A"
FT /id="PRO_0000429750"
FT DOMAIN 23..220
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT ACT_SITE 111
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT ACT_SITE 207
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 221 AA; 23813 MW; FAE314DCE529BF7B CRC64;
MKFATVLAFA TAAGAAFASP LASSETTEAG QLSKRQSINY VQNYNGNAAN FKYDQHAGTY
STRWTNPPDF VVGLGWSPGN SYRTIKFSGS YSSSSSSYSA VYGWLNNPLT EYYVVENYSY
DPCSNSGAQV VGSVTSDGSN YKICKHTQYD QPSIQGTKTF GQYFSVRANK RNSGSVTLSK
HFNAWKQHGF ANGAANPDFN YQVFATEAFG GTGSASMSVS G
