GUN_ASPAC
ID GUN_ASPAC Reviewed; 237 AA.
AC P22669;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Endoglucanase-1;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase;
DE AltName: Full=Endo-1,4-beta-glucanase;
DE AltName: Full=Endoglucanase I;
DE AltName: Full=FI-CMCase;
DE Flags: Precursor;
OS Aspergillus aculeatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5053;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=F-50;
RX PubMed=2216782; DOI=10.1093/nar/18.19.5884;
RA Ooi T., Shinmyo A., Okada H., Murao S., Kawaguchi T., Arai M.;
RT "Complete nucleotide sequence of a gene coding for Aspergillus aculeatus
RT cellulase (FI-CMCase).";
RL Nucleic Acids Res. 18:5884-5884(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND PYROGLUTAMATE
RP FORMATION AT GLN-17.
RC STRAIN=F-50;
RX PubMed=2249253; DOI=10.1007/bf00318384;
RA Ooi T., Shinmyo A., Okada H., Hara S., Ikenaka T., Murao S., Arai M.;
RT "Cloning and sequence analysis of a cDNA for cellulase (FI-CMCase) from
RT Aspergillus aculeatus.";
RL Curr. Genet. 18:217-222(1990).
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 -!- INDUCTION: By cellulosic materials and hemicelluloses.
CC -!- MISCELLANEOUS: Will also hydrolyze 1,4-linkages in beta-D-glucans also
CC containing 1,3-linkages.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 12 (cellulase H) 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; D00546; BAA00435.1; -; Genomic_DNA.
DR EMBL; X52525; CAA36757.1; -; mRNA.
DR PIR; S12610; S12610.
DR PDB; 5GM3; X-ray; 1.59 A; A/B=19-237.
DR PDB; 5GM4; X-ray; 1.92 A; A/B/C/D/E/F/G=19-237.
DR PDB; 5GM5; X-ray; 1.73 A; A/B/C/D/E/F/G=18-237.
DR PDBsum; 5GM3; -.
DR PDBsum; 5GM4; -.
DR PDBsum; 5GM5; -.
DR AlphaFoldDB; P22669; -.
DR SMR; P22669; -.
DR CAZy; GH12; Glycoside Hydrolase Family 12.
DR VEuPathDB; FungiDB:ASPACDRAFT_126244; -.
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; 2.60.120.180; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013319; GH11/12.
DR InterPro; IPR002594; GH12.
DR PANTHER; PTHR34002; PTHR34002; 1.
DR Pfam; PF01670; Glyco_hydro_12; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW Direct protein sequencing; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Pyrrolidone carboxylic acid; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..237
FT /note="Endoglucanase-1"
FT /id="PRO_0000008018"
FT MOD_RES 17
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:2249253"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:5GM3"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:5GM3"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:5GM3"
FT STRAND 45..56
FT /evidence="ECO:0007829|PDB:5GM3"
FT STRAND 61..71
FT /evidence="ECO:0007829|PDB:5GM3"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:5GM3"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:5GM3"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:5GM3"
FT STRAND 110..123
FT /evidence="ECO:0007829|PDB:5GM3"
FT STRAND 132..142
FT /evidence="ECO:0007829|PDB:5GM3"
FT STRAND 148..157
FT /evidence="ECO:0007829|PDB:5GM3"
FT STRAND 160..169
FT /evidence="ECO:0007829|PDB:5GM3"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:5GM3"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:5GM3"
FT HELIX 191..201
FT /evidence="ECO:0007829|PDB:5GM3"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:5GM3"
FT STRAND 209..234
FT /evidence="ECO:0007829|PDB:5GM3"
SQ SEQUENCE 237 AA; 25560 MW; 8F173571A8AE6931 CRC64;
MKAFHLLAAL AGAAVAQQAQ LCDQYATYTG GVYTINNNLW GKDAGSGSQC TTVNSASSAG
TSWSTKWNWS GGENSVKSYA NSGLTFNKKL VSQISQIPTT ARWSYDNTGI RADVAYDLFT
AADINHVTWS GDYELMIWLA RYGGVQPIGS QIATATVDGQ TWELWYGANG SQKTYSFVAP
TPITSFQGDV NDFFKYLTQN HGFPASSQYL ITLQFGTEPF TGGPATLSVS NWSASVQ
