P10477 (GUNE_CLOTM) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endoglucanase E
EC=3.2.1.4

Alternative name(s):
Cellulase E
Endo-1,4-beta-glucanase E
Short name=EgE

Gene names

Name:

celE

Organism

Clostridium thermocellum

Taxonomic identifier

1515 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	814 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Catalytic activity	Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Domain	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 similarities	Belongs to the glycosyl hydrolase 5 (cellulase A) family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Domain	Repeat Signal
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW lipid metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro cellulase activity Inferred from electronic annotation. Source: EC hydrolase activity, acting on ester bonds Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 34

34

Ref.1

Chain

35 – 814

780

Endoglucanase E

PRO_0000007852

Regions

Repeat

415 – 438

24

1

Repeat

451 – 474

24

2

Region

415 – 474

60

2 X 24 AA approximate repeats

Sites

Active site

193

1

Proton donor By similarity

Active site

316

1

Nucleophile By similarity

Secondary structure

1

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814

Helix Strand Turn

Details...

Beta strand

493 – 495

3

Beta strand

514 – 519

6

Beta strand

524 – 530

7

Beta strand

533 – 540

8

Beta strand

548 – 560

13

Beta strand

568 – 574

7

Beta strand

583 – 585

3

Beta strand

605 – 609

5

Helix

612 – 615

4

Helix

630 – 632

3

Helix

635 – 637

3

Helix

639 – 646

8

Beta strand

650 – 653

4

Helix

673 – 676

4

Beta strand

679 – 681

3

Helix

690 – 692

3

Beta strand

696 – 700

5

Turn

705 – 707

3

Beta strand

708 – 710

3

Helix

714 – 731

18

Beta strand

736 – 741

6

Helix

751 – 766

16

Beta strand

772 – 776

5

Helix

794 – 811

18

Sequences

	Sequence		Length	Mass (Da)
	P10477 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: C6FA24B8D1523632	FASTA	814	90,244
	10 20 30 40 50 60 MKKIVSLVCV LVMLVSILGS FSVVAASPVK GFQVSGTKLL DASGNELVMR GMRDISAIDL 70 80 90 100 110 120 VKEIKIGWNL GNTLDAPTET AWGNPRTTKA MIEKVREMGF NAVRVPVTWD THIGPAPDYK 130 140 150 160 170 180 IDEAWLNRVE EVVNYVLDCG MYAIINLHHD NTWIIPTYAN EQRSKEKLVK VWEQIATRFK 190 200 210 220 230 240 DYDDHLLFET MNEPREVGSP MEWMGGTYEN RDVINRFNLA VVNTIRASGG NNDKRFILVP 250 260 270 280 290 300 TNAATGLDVA LNDLVIPNND SRVIVSIHAY SPYFFAMDVN GTSYWGSDYD KASLTSELDA 310 320 330 340 350 360 IYNRFVKNGR AVIIGEFGTI DKNNLSSRVA HAEHYAREAV SRGIAVFWWD NGYYNPGDAE 370 380 390 400 410 420 TYALLNRKTL SWYYPEIVQA LMRGAGVEPL VSPTPTPTLM PTPSPTVTAN ILYGDVNGDG 430 440 450 460 470 480 KINSTDCTML KRYILRGIEE FPSPSGIIAA DVNADLKINS TDLVLMKKYL LRSIDKFPAE 490 500 510 520 530 540 DSQTPDEDNP GILYNGRFDF SDPNGPKCAW SGSNVELNFY GTEASVTIKS GGENWFQAIV 550 560 570 580 590 600 DGNPLPPFSV NATTSTVKLV SGLAEGAHHL VLWKRTEASL GEVQFLGFDF GSGKLLAAPK 610 620 630 640 650 660 PLERKIEFIG DSITCAYGNE GTSKEQSFTP KNENSYMSYA AITARNLNAS ANMIAWSGIG 670 680 690 700 710 720 LTMNYGGAPG PLIMDRYPYT LPYSGVRWDF SKYVPQVVVI NLGTNDFSTS FADKTKFVTA 730 740 750 760 770 780 YKNLISEVRR NYPDAHIFCC VGPMLWGTGL DLCRSYVTEV VNDCNRSGDL KVYFVEFPQQ 790 800 810 DGSTGYGEDW HPSIATHQLM AERLTAEIKN KLGW

References

[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: 3066698] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 35-58.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M22759 Genomic DNA. Translation: AAA23224.1.

PIR

CZCLEM. JT0347.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2WAB	X-ray	1.90	A	485-814	[»]
2WAO	X-ray	1.80	A	485-814	[»]

ProteinModelPortal

P10477.

ModBase

Search...

Protein family/group databases

CAZy

GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR013830. Esterase_SGNH_hydro-type.
IPR013831. Esterase_SGNH_hydro-type_subgr.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
IPR001087. Lipase_GDSL.
[Graphical view]

Gene3D

G3DSA:1.10.1330.10. Cellulos_enz_dockerin_1. 1 hit.
G3DSA:3.40.50.1110. Esterase_SGNH_hydro-type_subgr. 2 hits.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

Pfam

PF00150. Cellulase. 1 hit.
PF00404. Dockerin_1. 2 hits.
PF00657. Lipase_GDSL. 1 hit.
[Graphical view]

SUPFAM

SSF63446. Cellulos_enz_dockerin_1. 1 hit.
SSF52266. Esterase_SGNH_hydro-type. 1 hit.
SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GUNE_CLOTM

Accession

Primary (citable) accession number: P10477

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	September 21, 2011
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program