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Protein

Endoglucanase E1

Gene

Acel_0614

Organism
Acidothermus cellulolyticus (strain ATCC 43068 / 11B)
Status
Reviewed-Annotation score: Annotation score: 4 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)DescriptionActionsGraphical viewLength
Active sitei203Proton donor1
Active sitei323Nucleophile1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

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 lineageiBacteriaActinobacteriaAcidothermalesAcidothermaceaeAcidothermus
Proteomesi
  • UP000008221 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 41Add BLAST41
ChainiPRO_000000783442 – 562Endoglucanase E1Add BLAST521

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi75 ↔ 161
Disulfide bondi209 ↔ 212

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi351607.Acel_0614.

Structurei

Secondary structure

1562
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi48 – 50Combined sources3
Beta strandi53 – 55Combined sources3
Beta strandi65 – 68Combined sources4
Turni80 – 84Combined sources5
Helixi87 – 96Combined sources10
Beta strandi101 – 107Combined sources7
Helixi108 – 111Combined sources4
Beta strandi123 – 125Combined sources3
Turni127 – 131Combined sources5
Helixi134 – 147Combined sources14
Beta strandi151 – 160Combined sources10
Beta strandi166 – 168Combined sources3
Beta strandi171 – 173Combined sources3
Helixi175 – 188Combined sources14
Turni189 – 191Combined sources3
Beta strandi195 – 199Combined sources5
Beta strandi209 – 211Combined sources3
Turni215 – 217Combined sources3
Helixi219 – 233Combined sources15
Beta strandi237 – 242Combined sources6
Beta strandi244 – 247Combined sources4
Turni254 – 256Combined sources3
Turni259 – 263Combined sources5
Beta strandi269 – 272Combined sources4
Beta strandi274 – 279Combined sources6
Turni283 – 285Combined sources3
Helixi289 – 291Combined sources3
Turni294 – 299Combined sources6
Helixi300 – 307Combined sources8
Helixi309 – 313Combined sources5
Beta strandi319 – 323Combined sources5
Helixi331 – 343Combined sources13
Helixi347 – 350Combined sources4
Beta strandi356 – 360Combined sources5
Turni367 – 369Combined sources3
Beta strandi377 – 380Combined sources4
Helixi382 – 388Combined sources7
Helixi389 – 391Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ECEX-ray2.40A/B42-399[»]
1VRXX-ray2.40A/B42-399[»]
ProteinModelPortaliP54583.
SMRiP54583.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54583.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini458 – 562CBM2PROSITE-ProRule annotationAdd BLAST105

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni42 – 400CatalyticAdd BLAST359

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi401 – 461Pro/Ser/Thr-rich (linker)Add BLAST61

Sequence similaritiesi

Contains 1 CBM2 (carbohydrate binding type-2) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4106R7G. Bacteria.
COG2730. LUCA.
HOGENOMiHOG000225207.
KOiK01179.
OMAiTHGRATH.
OrthoDBiPOG091H1DNW.

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR008965. Carb-bd_dom.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
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

        10         20         30         40         50
MPRALRRVPG SRVMLRVGVV VAVLALVAAL ANLAVPRPAR AAGGGYWHTS
60 70 80 90 100
GREILDANNV PVRIAGINWF GFETCNYVVH GLWSRDYRSM LDQIKSLGYN
110 120 130 140 150
TIRLPYSDDI LKPGTMPNSI NFYQMNQDLQ GLTSLQVMDK IVAYAGQIGL
160 170 180 190 200
RIILDRHRPD CSGQSALWYT SSVSEATWIS DLQALAQRYK GNPTVVGFDL
210 220 230 240 250
HNEPHDPACW GCGDPSIDWR LAAERAGNAV LSVNPNLLIF VEGVQSYNGD
260 270 280 290 300
SYWWGGNLQG AGQYPVVLNV PNRLVYSAHD YATSVYPQTW FSDPTFPNNM
310 320 330 340 350
PGIWNKNWGY LFNQNIAPVW LGEFGTTLQS TTDQTWLKTL VQYLRPTAQY
360 370 380 390 400
GADSFQWTFW SWNPDSGDTG GILKDDWQTV DTVKDGYLAP IKSSIFDPVG
410 420 430 440 450
ASASPSSQPS PSVSPSPSPS PSASRTPTPT PTPTASPTPT LTPTATPTPT
460 470 480 490 500
ASPTPSPTAA SGARCTASYQ VNSDWGNGFT VTVAVTNSGS VATKTWTVSW
510 520 530 540 550
TFGGNQTITN SWNAAVTQNG QSVTARNMSY NNVIQPGQNT TFGFQASYTG
560
SNAAPTVACA AS
Length:562
Mass (Da):60,748
Last modified:October 1, 1996 - v1
Checksum:i84E6256406A35041
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33212 Genomic DNA. Translation: AAA75477.1.
CP000481 Genomic DNA. Translation: ABK52387.1.
RefSeqiWP_011719450.1. NC_008578.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33212 Genomic DNA. Translation: AAA75477.1.
CP000481 Genomic DNA. Translation: ABK52387.1.
RefSeqiWP_011719450.1. NC_008578.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ECEX-ray2.40A/B42-399[»]
1VRXX-ray2.40A/B42-399[»]
ProteinModelPortaliP54583.
SMRiP54583.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi351607.Acel_0614.

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4106R7G. Bacteria.
COG2730. LUCA.
HOGENOMiHOG000225207.
KOiK01179.
OMAiTHGRATH.
OrthoDBiPOG091H1DNW.

Miscellaneous databases

EvolutionaryTraceiP54583.

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR008965. Carb-bd_dom.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
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]
ProtoNetiSearch...

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: November 2, 2016
This is version 110 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, Reference 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.