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P54583

- GUN1_ACIC1

UniProt

P54583 - GUN1_ACIC1

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Protein
Endoglucanase E1
Gene
Acel_0614
Organism
Acidothermus cellulolyticus (strain ATCC 43068 / 11B)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Has a very high specific activity on carboxymethylcellulose.

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Temperature dependencei

Optimum temperature is 81 degrees Celsius. Thermostable.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei203 – 2031Proton donor
Active sitei323 – 3231Nucleophile

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB-EC
  2. polysaccharide binding Source: InterPro

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciACEL351607:GIXW-627-MONOMER.

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
GH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase E1 (EC:3.2.1.4)
Alternative name(s):
Cellulase E1
Endo-1,4-beta-glucanase E1
Endocellulase E1
Gene namesi
Ordered Locus Names:Acel_0614
OrganismiAcidothermus cellulolyticus (strain ATCC 43068 / 11B)
Taxonomic identifieri351607 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesFrankineaeAcidothermaceaeAcidothermus
ProteomesiUP000008221: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4141
Add
BLAST
Chaini42 – 562521Endoglucanase E1
PRO_0000007834Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi75 ↔ 161
Disulfide bondi209 ↔ 212

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi351607.Acel_0614.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi48 – 503
Beta strandi53 – 553
Beta strandi65 – 684
Turni80 – 845
Helixi87 – 9610
Beta strandi101 – 1077
Helixi108 – 1114
Beta strandi123 – 1253
Turni127 – 1315
Helixi134 – 14714
Beta strandi151 – 16010
Beta strandi166 – 1683
Beta strandi171 – 1733
Helixi175 – 18814
Turni189 – 1913
Beta strandi195 – 1995
Beta strandi209 – 2113
Turni215 – 2173
Helixi219 – 23315
Beta strandi237 – 2426
Beta strandi244 – 2474
Turni254 – 2563
Turni259 – 2635
Beta strandi269 – 2724
Beta strandi274 – 2796
Turni283 – 2853
Helixi289 – 2913
Turni294 – 2996
Helixi300 – 3078
Helixi309 – 3135
Beta strandi319 – 3235
Helixi331 – 34313
Helixi347 – 3504
Beta strandi356 – 3605
Turni367 – 3693
Beta strandi377 – 3804
Helixi382 – 3887
Helixi389 – 3913

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ECEX-ray2.40A/B42-399[»]
1VRXX-ray2.40A/B42-399[»]
ProteinModelPortaliP54583.
SMRiP54583. Positions 42-399.

Miscellaneous databases

EvolutionaryTraceiP54583.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini458 – 562105CBM2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni42 – 400359Catalytic
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi401 – 46161Pro/Ser/Thr-rich (linker)
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000225207.
KOiK01179.
OMAiNSWGMRC.
OrthoDBiEOG6FRCSN.

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTiSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P54583-1 [UniParc]FASTAAdd to Basket

« Hide

MPRALRRVPG SRVMLRVGVV VAVLALVAAL ANLAVPRPAR AAGGGYWHTS    50
GREILDANNV PVRIAGINWF GFETCNYVVH GLWSRDYRSM LDQIKSLGYN 100
TIRLPYSDDI LKPGTMPNSI NFYQMNQDLQ GLTSLQVMDK IVAYAGQIGL 150
RIILDRHRPD CSGQSALWYT SSVSEATWIS DLQALAQRYK GNPTVVGFDL 200
HNEPHDPACW GCGDPSIDWR LAAERAGNAV LSVNPNLLIF VEGVQSYNGD 250
SYWWGGNLQG AGQYPVVLNV PNRLVYSAHD YATSVYPQTW FSDPTFPNNM 300
PGIWNKNWGY LFNQNIAPVW LGEFGTTLQS TTDQTWLKTL VQYLRPTAQY 350
GADSFQWTFW SWNPDSGDTG GILKDDWQTV DTVKDGYLAP IKSSIFDPVG 400
ASASPSSQPS PSVSPSPSPS PSASRTPTPT PTPTASPTPT LTPTATPTPT 450
ASPTPSPTAA SGARCTASYQ VNSDWGNGFT VTVAVTNSGS VATKTWTVSW 500
TFGGNQTITN SWNAAVTQNG QSVTARNMSY NNVIQPGQNT TFGFQASYTG 550
SNAAPTVACA AS 562
Length:562
Mass (Da):60,748
Last modified:October 1, 1996 - v1
Checksum:i84E6256406A35041
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U33212 Genomic DNA. Translation: AAA75477.1.
CP000481 Genomic DNA. Translation: ABK52387.1.
RefSeqiWP_011719450.1. NC_008578.1.
YP_872373.1. NC_008578.1.

Genome annotation databases

EnsemblBacteriaiABK52387; ABK52387; Acel_0614.
GeneIDi4486396.
KEGGiace:Acel_0614.
PATRICi20671622. VBIAciCel132453_0657.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U33212 Genomic DNA. Translation: AAA75477.1 .
CP000481 Genomic DNA. Translation: ABK52387.1 .
RefSeqi WP_011719450.1. NC_008578.1.
YP_872373.1. NC_008578.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ECE X-ray 2.40 A/B 42-399 [» ]
1VRX X-ray 2.40 A/B 42-399 [» ]
ProteinModelPortali P54583.
SMRi P54583. Positions 42-399.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 351607.Acel_0614.

Protein family/group databases

CAZyi CBM2. Carbohydrate-Binding Module Family 2.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABK52387 ; ABK52387 ; Acel_0614 .
GeneIDi 4486396.
KEGGi ace:Acel_0614.
PATRICi 20671622. VBIAciCel132453_0657.

Phylogenomic databases

eggNOGi COG2730.
HOGENOMi HOG000225207.
KOi K01179.
OMAi NSWGMRC.
OrthoDBi EOG6FRCSN.

Enzyme and pathway databases

BioCyci ACEL351607:GIXW-627-MONOMER.

Miscellaneous databases

EvolutionaryTracei P54583.

Family and domain databases

Gene3Di 2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00553. CBM_2. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view ]
SMARTi SM00637. CBD_II. 1 hit.
[Graphical view ]
SUPFAMi SSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEi PS51173. CBM2. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Laymon R.A., Himmel M.E., Thomas S.R.
    Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43068 / 11B.
  3. "Crystal structure of thermostable family 5 endocellulase E1 from Acidothermus cellulolyticus in complex with cellotetraose."
    Sakon J., Adney W.S., Himmel M.E., Thomas S.R., Kaplus P.A.
    Biochemistry 35:10648-10660(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 42-398.

Entry informationi

Entry nameiGUN1_ACIC1
AccessioniPrimary (citable) accession number: P54583
Secondary accession number(s): A0LSH7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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