Reviewed, UniProtKB/Swiss-Prot P17901 (GUNA_CLOCE)

Names and origin

Protein names

Recommended name:
    Endoglucanase A
    EC=3.2.1.4
Alternative name(s):
    Endo-1,4-beta-glucanase A
    Cellulase A
    EGCCA

Gene names

Name:	celCCA
Ordered Locus Names:	Ccel_1099

Organism

Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)

Taxonomic identifier

394503 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	475 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	The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
Catalytic activity	Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Domain	A 24 residues 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.
Miscellaneous	The C-terminus (AA 411-475) may play a role in organizing the cellulosome complex.
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
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro cellulase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

26

Ref.1

Chain

27 – 475

449

Endoglucanase A

PRO_0000007845

Regions

Repeat

415 – 438

24

1

Repeat

446 – 469

24

2

Region

415 – 469

55

2 X 24 AA approximate repeats

Sites

Active site

147

1

Probable

Active site

195

1

Proton donor

Active site

332

1

Nucleophile

Experimental info

Mutagenesis

104

1

R → K: Small loss of activity. Ref.4

Mutagenesis

104

1

R → S or V: Large decrease of activity. Ref.4

Mutagenesis

147

1

H → S, E, G or F: Total loss of activity. Ref.4

Mutagenesis

148

1

H → V: Large decrease of activity. Ref.4

Secondary structure

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475

Helix Strand Turn

Details...

Helix

29 – 31

3

Helix

46 – 54

9

Beta strand

56 – 59

4

Helix

75 – 77

3

Helix

78 – 81

4

Helix

89 – 98

10

Beta strand

102 – 105

4

Helix

110 – 112

3

Turn

115 – 118

4

Helix

122 – 136

15

Turn

137 – 139

3

Beta strand

141 – 145

5

Turn

152 – 154

3

Helix

160 – 162

3

Helix

163 – 180

18

Turn

181 – 183

3

Beta strand

188 – 191

4

Turn

202 – 205

4

Helix

212 – 234

23

Helix

237 – 240

4

Beta strand

244 – 247

4

Helix

249 – 251

3

Helix

253 – 257

5

Beta strand

274 – 279

6

Helix

284 – 287

4

Helix

291 – 293

3

Helix

304 – 320

17

Helix

322 – 324

3

Beta strand

328 – 333

6

Helix

341 – 357

17

Beta strand

361 – 364

4

Beta strand

371 – 374

4

Turn

382 – 385

4

Beta strand

386 – 389

4

Helix

390 – 399

10

Beta strand

418 – 420

3

Helix

424 – 435

12

Helix

443 – 445

3

Helix

455 – 465

11

Sequences

	Sequence		Length	Mass (Da)
	P17901-1 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: 1AF20EA2C0A132F9	FASTA	475	53,625
	10 20 30 40 50 60 MKKTTAFLLC FLMIFTALLP MQNANAYDAS LIPNLQIPQK NIPNNDGMNF VKGLRLGWNL 70 80 90 100 110 120 GNTFDAFNGT NITNELDYET SWSGIKTTKQ MIDAIKQKGF NTVRIPVSWH PHVSGSDYKI 130 140 150 160 170 180 SDVWMNRVQE VVNYCIDNKM YVILNTHHDV DKVKGYFPSS QYMASSKKYI TSVWAQIAAR 190 200 210 220 230 240 FANYDEHLIF EGMNEPRLVG HANEWWPELT NSDVVDSINC INQLNQDFVN TVRATGGKNA 250 260 270 280 290 300 SRYLMCPGYV ASPDGATNDY FRMPNDISGN NNKIIVSVHA YCPWNFAGLA MADGGTNAWN 310 320 330 340 350 360 INDSKDQSEV TWFMDNIYNK YTSRGIPVII GECGAVDKNN LKTRVEYMSY YVAQAKARGI 370 380 390 400 410 420 LCILWDNNNF SGTGELFGFF DRRSCQFKFP EIIDGMVKYA FEAKTDPDPV IVYGDYNNDG 430 440 450 460 470 NVDALDFAGL KKYIMAADHA YVKNLDVNLD NEVNAFDLAI LKKYLLGMVS KLPSN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of the Clostridium cellulolyticum endoglucanase-A-encoding gene, celCCA." Faure E., Belaich A., Bagnara C., Gaudin C., Belaich J.-P. Gene 84:39-46(1989) [PubMed: 2558058] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-39.
[2]	"Complete sequence of Clostridium cellulolyticum H10." Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N. , Ivanova N., Zhou J., Richardson P. Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Characterization of endoglucanase A from Clostridium cellulolyticum." Fierobe H.-P., Gaudin C., Belaich A., Loufti M., Faure E., Bagnara C., Baty D., Belaich J.-P. J. Bacteriol. 173:7956-7962(1991) [PubMed: 1744052] [Abstract] Cited for: CHARACTERIZATION.
[4]	"The catalytic domain of endoglucanase A from Clostridium cellulolyticum: effects of arginine 79 and histidine 122 mutations on catalysis." Belaich A., Fierobe H.-P., Baty D., Busetta B., Bagnara-Tardif C., Gaudin C., Belaich J.-P. J. Bacteriol. 174:4677-4682(1992) [PubMed: 1624455] [Abstract] Cited for: MUTAGENESIS OF ARG-104; HIS-147 AND HIS-148.
[5]	"Crystal structure of the catalytic domain of a bacterial cellulase belonging to family 5." Ducros V., Czjzek M., Belaich A., Gaudin C., Fierobe H.P., Belaich J.-P., Davies G.J., Haser R. Structure 3:939-949(1995) [PubMed: 8535787] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 27-406.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M93096 Genomic DNA. Translation: AAA51444.1.
M32362 Genomic DNA. Translation: AAA23221.1.
CP001348 Genomic DNA. Translation: ACL75458.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EDG	X-ray	1.60	A	27-401	[»]
2VN5	X-ray	1.90	B/D	410-475	[»]
2VN6	X-ray	1.49	B	410-472	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH5. Glycoside Hydrolase Family 5.

Enzyme and pathway databases

BRENDA

3.2.1.4. 97402.

Family and domain databases

InterPro

IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR018247. EF_HAND_1.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]

Gene3D

G3DSA:1.10.1330.10. Cellulos_enz_dockerin_1. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

Pfam

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

PROSITE

PS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 1 hit. Uncertain.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GUNA_CLOCE

Accession

Primary (citable) accession number: P17901
Secondary accession number(s): B8HZV8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	June 16, 2009
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)