GUN1_USTMA
ID GUN1_USTMA Reviewed; 393 AA.
AC P54424; A0A0D1CA77; Q4P0N1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Endoglucanase 1;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase 1;
DE AltName: Full=Endo-1,4-beta-glucanase 1;
DE Short=EG 1;
DE Flags: Precursor;
GN Name=EGL1; ORFNames=UMAG_06332;
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 [GENOMIC DNA].
RC STRAIN=FBD11;
RX PubMed=8590631; DOI=10.1515/bchm3.1995.376.10.617;
RA Schauwecker F., Wanner G., Kahmann R.;
RT "Filament-specific expression of a cellulase gene in the dimorphic fungus
RT Ustilago maydis.";
RL Biol. Chem. Hoppe-Seyler 376:617-625(1995).
RN [2]
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 [3]
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.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Hyphal tip.
CC -!- DEVELOPMENTAL STAGE: Expressed in filamentous dikaryon.
CC -!- PTM: May also be O-glycosylated.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 45 (cellulase K) family.
CC {ECO:0000305}.
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DR EMBL; S81598; AAB36147.1; -; Genomic_DNA.
DR EMBL; CM003143; KIS70247.1; -; Genomic_DNA.
DR PIR; S59499; S59499.
DR RefSeq; XP_011388317.1; XM_011390015.1.
DR AlphaFoldDB; P54424; -.
DR SMR; P54424; -.
DR CAZy; GH45; Glycoside Hydrolase Family 45.
DR CLAE; EGL45A_USTMA; -.
DR EnsemblFungi; KIS70247; KIS70247; UMAG_06332.
DR GeneID; 23565950; -.
DR KEGG; uma:UMAG_06332; -.
DR VEuPathDB; FungiDB:UMAG_06332; -.
DR eggNOG; ENOG502QTGS; Eukaryota.
DR HOGENOM; CLU_045022_0_0_1; -.
DR InParanoid; P54424; -.
DR OMA; MIVQASN; -.
DR OrthoDB; 1103094at2759; -.
DR BioCyc; MetaCyc:MON-17192; -.
DR Proteomes; UP000000561; Chromosome 4.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.40.40.10; -; 1.
DR InterPro; IPR000334; Glyco_hydro_45.
DR InterPro; IPR036908; RlpA-like_sf.
DR Pfam; PF02015; Glyco_hydro_45; 1.
DR SUPFAM; SSF50685; SSF50685; 1.
DR PROSITE; PS01140; GLYCOSYL_HYDROL_F45; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..393
FT /note="Endoglucanase 1"
FT /id="PRO_0000008025"
FT REGION 233..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 34
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10069"
FT ACT_SITE 152
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 393 AA; 39594 MW; 65C753C610CD6AD3 CRC64;
MAFKLNIGLL ALSLSLSLVH LDGVRAGMAT RYWDCCLASA SWEGKAPVYA PVDACKADGV
TLIDSKKDPS GQSGCNGGNK FMCSCMQPFD DETDPTLAFG FGAFTTGQES DTDCACFYAE
FEHDAQGKAM KRNKLIFQVT NVGGDVQSQN FDFQIPGGGL GAFPKGCPAQ WGVEASLWGD
QYGGVKSATE CSKLPKPLQE GCKWRFSEWG DNPVLKGSPK RVKCPKSLID RSGCQRKDDN
TISPYSGKVD SANTAAPAQY KRDRSVCLAG GKKGKSAAGG VDGSGDASGG ADASGAGGAA
EGSQGQPEGY GQPSGGNDQG SSNGDATTGA GSGSGSDSGS TANGSGSGAP TSGSDGSAVA
PPSGGSNPGA AQGGQGGAQP GPSGGHKKCH KKH
