GUN_ROBSP
ID GUN_ROBSP Reviewed; 385 AA.
AC P23044; Q9P981;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Endoglucanase 1;
DE EC=3.2.1.4;
DE AltName: Full=Carboxymethyl-cellulase I;
DE Short=CMCase I;
DE AltName: Full=Endo-1,4-beta-glucanase;
DE AltName: Full=Endoglucanase I;
DE Flags: Precursor;
GN Name=eg 1;
OS Robillarda sp. (strain Y-20).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Robillarda;
OC unclassified Robillarda.
OX NCBI_TaxID=72589;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kashiwagi Y.;
RT "Endoglucanase gene from cellulolytic fungi, Robillarda sp. Y-20.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-385, AND PROTEIN SEQUENCE OF 18-35.
RX PubMed=2277031; DOI=10.1093/oxfordjournals.jbchem.a123211;
RA Yoshigi N., Taniguchi H., Sasaki T.;
RT "Cloning and sequencing of the endo-cellulase cDNA from Robillarda sp. Y-
RT 20.";
RL J. Biochem. 108:388-392(1990).
CC -!- FUNCTION: Active towards carboxymethyl cellulose.
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 -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=Ref.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB030819; BAA90480.1; -; Genomic_DNA.
DR AlphaFoldDB; P23044; -.
DR SMR; P23044; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR CLAE; EGL5A_ROBSP; -.
DR UniPathway; UPA00696; -.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:2277031"
FT CHAIN 18..385
FT /note="Endoglucanase 1"
FT /id="PRO_0000184049"
FT ACT_SITE 176
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 284
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 27..28
FT /note="SS -> GN (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 41428 MW; 149604D42369AD33 CRC64;
MKLVFSALAS LLSGASATIY YAGVAESSGE FGVWSATQTP GTGLPGRFGV DYAFISEAAV
DVHVDQNHLN LFRVAFLLER MCPPATGLGA AFNETHFDYF KEAVDYITVT KGAYAILDPH
NYMRYNDPSY QPFSGSVIGN TSDSTAATTE QFGEFWGELA SRFNDNERVI FGLMNEPHDM
ATSLVLANNQ AAIDAIRAAN ASNLIIMPGN SWTGGHSWTE GSDPSSALLN QFKDPLNNTA
IDIHEYLDYD FSGGHLECVS DPETNLAALT AWLKENNLKA FITEFGGSNS TSCQEMLPDL
INYMADNAEY IGWTAWAAGP FWGPNSPCCT NSTQLGSLEP GSTAVDGSPG LYDTVWLPVI
QPLVPTELQW SGPASISGGE LTSRA
