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P10477

- GUNE_CLOTM

UniProt

P10477 - GUNE_CLOTM

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Protein

Endoglucanase E

Gene

celE

Organism
Clostridium thermocellum (Ruminiclostridium thermocellum)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei193 – 1931Proton donorBy similarity
Active sitei316 – 3161NucleophileBy similarity

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB-EC
  2. hydrolase activity, acting on ester bonds Source: InterPro

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
  2. lipid metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase E (EC:3.2.1.4)
Alternative name(s):
Cellulase E
Endo-1,4-beta-glucanase E
Short name:
EgE
Gene namesi
Name:celE
OrganismiClostridium thermocellum (Ruminiclostridium thermocellum)
Taxonomic identifieri1515 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 34341 PublicationAdd
BLAST
Chaini35 – 814780Endoglucanase EPRO_0000007852Add
BLAST

Structurei

Secondary structure

1
814
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi57 – 648
Beta strandi66 – 705
Beta strandi76 – 783
Turni79 – 824
Helixi89 – 979
Beta strandi102 – 1054
Helixi110 – 1123
Turni116 – 1183
Helixi123 – 13816
Beta strandi142 – 1454
Turni151 – 1533
Turni158 – 1603
Helixi161 – 17818
Turni179 – 1813
Beta strandi186 – 1905
Turni200 – 2056
Helixi208 – 22619
Turni230 – 2345
Beta strandi237 – 2393
Helixi242 – 2443
Helixi248 – 2514
Helixi257 – 2593
Beta strandi263 – 2686
Helixi273 – 2764
Helixi288 – 30417
Helixi306 – 3083
Beta strandi312 – 3176
Helixi325 – 34016
Turni341 – 3433
Beta strandi345 – 3506
Turni367 – 3704
Beta strandi371 – 3733
Helixi375 – 38511
Beta strandi493 – 4964
Beta strandi514 – 5229
Beta strandi524 – 54017
Beta strandi548 – 56013
Beta strandi565 – 57410
Helixi578 – 5803
Beta strandi583 – 5897
Beta strandi593 – 5953
Beta strandi603 – 6119
Helixi612 – 6154
Turni616 – 6205
Helixi630 – 6323
Helixi635 – 6373
Helixi639 – 6468
Beta strandi649 – 6557
Helixi665 – 6673
Helixi673 – 6764
Beta strandi679 – 6813
Turni682 – 6854
Helixi690 – 6923
Beta strandi696 – 7016
Helixi704 – 7074
Beta strandi708 – 7103
Helixi714 – 73118
Beta strandi736 – 7416
Helixi747 – 76620
Beta strandi771 – 7766
Helixi788 – 7903
Helixi794 – 81219

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WABX-ray1.90A485-814[»]
2WAOX-ray1.80A485-814[»]
4IM4X-ray2.42A/B/C/D/E/F51-386[»]
ProteinModelPortaliP10477.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10477.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati415 – 438241Add
BLAST
Repeati451 – 474242Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni415 – 474602 X 24 AA approximate repeatsAdd
BLAST

Domaini

A 24 residue domain is repeated twice in this enzyme as well as in other C.thermocellum cellulosome enzymes. This domain may function as the binding ligand for the SL component.

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di1.10.1330.10. 1 hit.
3.20.20.80. 1 hit.
3.40.50.1110. 1 hit.
InterProiIPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR001087. Lipase_GDSL.
IPR013831. SGNH_hydro-type_esterase_dom.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
PF00404. Dockerin_1. 2 hits.
PF00657. Lipase_GDSL. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P10477 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKKIVSLVCV LVMLVSILGS FSVVAASPVK GFQVSGTKLL DASGNELVMR
60 70 80 90 100
GMRDISAIDL VKEIKIGWNL GNTLDAPTET AWGNPRTTKA MIEKVREMGF
110 120 130 140 150
NAVRVPVTWD THIGPAPDYK IDEAWLNRVE EVVNYVLDCG MYAIINLHHD
160 170 180 190 200
NTWIIPTYAN EQRSKEKLVK VWEQIATRFK DYDDHLLFET MNEPREVGSP
210 220 230 240 250
MEWMGGTYEN RDVINRFNLA VVNTIRASGG NNDKRFILVP TNAATGLDVA
260 270 280 290 300
LNDLVIPNND SRVIVSIHAY SPYFFAMDVN GTSYWGSDYD KASLTSELDA
310 320 330 340 350
IYNRFVKNGR AVIIGEFGTI DKNNLSSRVA HAEHYAREAV SRGIAVFWWD
360 370 380 390 400
NGYYNPGDAE TYALLNRKTL SWYYPEIVQA LMRGAGVEPL VSPTPTPTLM
410 420 430 440 450
PTPSPTVTAN ILYGDVNGDG KINSTDCTML KRYILRGIEE FPSPSGIIAA
460 470 480 490 500
DVNADLKINS TDLVLMKKYL LRSIDKFPAE DSQTPDEDNP GILYNGRFDF
510 520 530 540 550
SDPNGPKCAW SGSNVELNFY GTEASVTIKS GGENWFQAIV DGNPLPPFSV
560 570 580 590 600
NATTSTVKLV SGLAEGAHHL VLWKRTEASL GEVQFLGFDF GSGKLLAAPK
610 620 630 640 650
PLERKIEFIG DSITCAYGNE GTSKEQSFTP KNENSYMSYA AITARNLNAS
660 670 680 690 700
ANMIAWSGIG LTMNYGGAPG PLIMDRYPYT LPYSGVRWDF SKYVPQVVVI
710 720 730 740 750
NLGTNDFSTS FADKTKFVTA YKNLISEVRR NYPDAHIFCC VGPMLWGTGL
760 770 780 790 800
DLCRSYVTEV VNDCNRSGDL KVYFVEFPQQ DGSTGYGEDW HPSIATHQLM
810
AERLTAEIKN KLGW
Length:814
Mass (Da):90,244
Last modified:July 1, 1989 - v1
Checksum:iC6FA24B8D1523632
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M22759 Genomic DNA. Translation: AAA23224.1.
PIRiJT0347. CZCLEM.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M22759 Genomic DNA. Translation: AAA23224.1 .
PIRi JT0347. CZCLEM.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2WAB X-ray 1.90 A 485-814 [» ]
2WAO X-ray 1.80 A 485-814 [» ]
4IM4 X-ray 2.42 A/B/C/D/E/F 51-386 [» ]
ProteinModelPortali P10477.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P10477.

Family and domain databases

Gene3Di 1.10.1330.10. 1 hit.
3.20.20.80. 1 hit.
3.40.50.1110. 1 hit.
InterProi IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR001087. Lipase_GDSL.
IPR013831. SGNH_hydro-type_esterase_dom.
[Graphical view ]
Pfami PF00150. Cellulase. 1 hit.
PF00404. Dockerin_1. 2 hits.
PF00657. Lipase_GDSL. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEi PS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Conserved reiterated domains in Clostridium thermocellum endoglucanases are not essential for catalytic activity."
    Hall J., Hazlewood G.P., Barker P.J., Gilbert H.J.
    Gene 69:29-38(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 35-58.

Entry informationi

Entry nameiGUNE_CLOTM
AccessioniPrimary (citable) accession number: P10477
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: October 1, 2014
This is version 91 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, Direct protein sequencing

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