GUN1_ACIC1
ID GUN1_ACIC1 Reviewed; 562 AA.
AC P54583; A0LSH7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Endoglucanase E1;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase E1;
DE AltName: Full=Endo-1,4-beta-glucanase E1;
DE AltName: Full=Endocellulase E1;
DE Flags: Precursor;
GN OrderedLocusNames=Acel_0614;
OS Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC Bacteria; Actinobacteria; Acidothermales; Acidothermaceae; Acidothermus.
OX NCBI_TaxID=351607;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Laymon R.A., Himmel M.E., Thomas S.R.;
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43068 / DSM 8971 / 11B;
RX PubMed=19270083; DOI=10.1101/gr.084848.108;
RA Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT "Complete genome of the cellulolytic thermophile Acidothermus
RT cellulolyticus 11B provides insights into its ecophysiological and
RT evolutionary adaptations.";
RL Genome Res. 19:1033-1043(2009).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 42-398.
RX PubMed=8718854; DOI=10.1021/bi9604439;
RA Sakon J., Adney W.S., Himmel M.E., Thomas S.R., Kaplus P.A.;
RT "Crystal structure of thermostable family 5 endocellulase E1 from
RT Acidothermus cellulolyticus in complex with cellotetraose.";
RL Biochemistry 35:10648-10660(1996).
CC -!- FUNCTION: Has a very high specific activity on carboxymethylcellulose.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 81 degrees Celsius. Thermostable.;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; U33212; AAA75477.1; -; Genomic_DNA.
DR EMBL; CP000481; ABK52387.1; -; Genomic_DNA.
DR RefSeq; WP_011719450.1; NC_008578.1.
DR PDB; 1ECE; X-ray; 2.40 A; A/B=42-399.
DR PDB; 1VRX; X-ray; 2.40 A; A/B=42-399.
DR PDBsum; 1ECE; -.
DR PDBsum; 1VRX; -.
DR AlphaFoldDB; P54583; -.
DR SMR; P54583; -.
DR STRING; 351607.Acel_0614; -.
DR DrugBank; DB02379; Beta-D-Glucose.
DR CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR EnsemblBacteria; ABK52387; ABK52387; Acel_0614.
DR KEGG; ace:Acel_0614; -.
DR eggNOG; COG2730; Bacteria.
DR HOGENOM; CLU_020735_1_0_11; -.
DR OMA; INWYGAS; -.
DR OrthoDB; 1395441at2; -.
DR EvolutionaryTrace; P54583; -.
DR Proteomes; UP000008221; Chromosome.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.290; -; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF49384; SSF49384; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW Disulfide bond; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Reference proteome; Signal.
FT SIGNAL 1..41
FT CHAIN 42..562
FT /note="Endoglucanase E1"
FT /id="PRO_0000007834"
FT DOMAIN 458..562
FT /note="CBM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT REGION 42..400
FT /note="Catalytic"
FT REGION 399..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..454
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 203
FT /note="Proton donor"
FT ACT_SITE 323
FT /note="Nucleophile"
FT DISULFID 75..161
FT DISULFID 209..212
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:1ECE"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1ECE"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:1ECE"
FT TURN 80..84
FT /evidence="ECO:0007829|PDB:1ECE"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:1ECE"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:1ECE"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:1ECE"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1ECE"
FT TURN 127..131
FT /evidence="ECO:0007829|PDB:1ECE"
FT HELIX 134..147
FT /evidence="ECO:0007829|PDB:1ECE"
FT STRAND 151..160
FT /evidence="ECO:0007829|PDB:1ECE"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:1ECE"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:1ECE"
FT HELIX 175..188
FT /evidence="ECO:0007829|PDB:1ECE"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:1ECE"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:1ECE"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:1ECE"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:1ECE"
FT HELIX 219..233
FT /evidence="ECO:0007829|PDB:1ECE"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:1ECE"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:1ECE"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:1ECE"
FT TURN 259..263
FT /evidence="ECO:0007829|PDB:1ECE"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:1ECE"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:1ECE"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:1ECE"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:1ECE"
FT TURN 294..299
FT /evidence="ECO:0007829|PDB:1ECE"
FT HELIX 300..307
FT /evidence="ECO:0007829|PDB:1ECE"
FT HELIX 309..313
FT /evidence="ECO:0007829|PDB:1ECE"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:1ECE"
FT HELIX 331..343
FT /evidence="ECO:0007829|PDB:1ECE"
FT HELIX 347..350
FT /evidence="ECO:0007829|PDB:1ECE"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:1ECE"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:1ECE"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:1ECE"
FT HELIX 382..388
FT /evidence="ECO:0007829|PDB:1ECE"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:1ECE"
SQ SEQUENCE 562 AA; 60748 MW; 84E6256406A35041 CRC64;
MPRALRRVPG SRVMLRVGVV VAVLALVAAL ANLAVPRPAR AAGGGYWHTS GREILDANNV
PVRIAGINWF GFETCNYVVH GLWSRDYRSM LDQIKSLGYN TIRLPYSDDI LKPGTMPNSI
NFYQMNQDLQ GLTSLQVMDK IVAYAGQIGL RIILDRHRPD CSGQSALWYT SSVSEATWIS
DLQALAQRYK GNPTVVGFDL HNEPHDPACW GCGDPSIDWR LAAERAGNAV LSVNPNLLIF
VEGVQSYNGD SYWWGGNLQG AGQYPVVLNV PNRLVYSAHD YATSVYPQTW FSDPTFPNNM
PGIWNKNWGY LFNQNIAPVW LGEFGTTLQS TTDQTWLKTL VQYLRPTAQY GADSFQWTFW
SWNPDSGDTG GILKDDWQTV DTVKDGYLAP IKSSIFDPVG ASASPSSQPS PSVSPSPSPS
PSASRTPTPT PTPTASPTPT LTPTATPTPT ASPTPSPTAA SGARCTASYQ VNSDWGNGFT
VTVAVTNSGS VATKTWTVSW TFGGNQTITN SWNAAVTQNG QSVTARNMSY NNVIQPGQNT
TFGFQASYTG SNAAPTVACA AS
