P28623 (GUND_CLOC7) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endoglucanase D
EC=3.2.1.4

Alternative name(s):
Cellulase D
Endo-1,4-beta-glucanase D

Gene names

Name:	engD
Ordered Locus Names:	Clocel_3242

Organism

Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) [Complete proteome] [HAMAP]

Taxonomic identifier

573061 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium › Clostridium cellulovorans

Protein attributes

Sequence length	515 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	Has endoglucanase activity on carboxymethyl-cellulose (CMC), cellobiosidase activity on p-nitrophenyl-cellobioside (p-NPC), and partial hydrolytic activity on crystalline cellulose (Avicel).
Catalytic activity	Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence similarities	Belongs to the glycosyl hydrolase 5 (cellulase A) family. Contains 1 CBM2 (carbohydrate binding type-2) domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological_process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	cellulase activity Inferred from electronic annotation. Source: EC polysaccharide binding 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 – 31

31

Ref.1

Chain

32 – 515

484

Endoglucanase D

PRO_0000007848

Regions

Domain

404 – 515

112

CBM2

Region

32 – 376

345

Catalytic By similarity

Compositional bias

377 – 407

31

Pro/Thr-rich (linker)

Sites

Active site

180

1

Proton donor By similarity

Active site

303

1

Nucleophile By similarity

Experimental info

Sequence conflict

188 – 189

2

NE → LQ in AAA23233. Ref.1

Secondary structure

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515

Helix Strand Turn

Details...

Helix

43 – 50

8

Helix

76 – 84

9

Beta strand

89 – 92

4

Turn

103 – 105

3

Helix

110 – 124

15

Turn

125 – 127

3

Beta strand

129 – 132

4

Turn

138 – 140

3

Turn

145 – 147

3

Helix

148 – 165

18

Turn

166 – 168

3

Beta strand

173 – 177

5

Turn

187 – 190

4

Helix

195 – 214

20

Turn

219 – 221

3

Beta strand

224 – 227

4

Helix

229 – 231

3

Helix

235 – 239

5

Helix

244 – 246

3

Beta strand

250 – 253

4

Helix

260 – 263

4

Helix

275 – 291

17

Turn

292 – 294

3

Beta strand

299 – 301

3

Helix

312 – 327

16

Beta strand

332 – 335

4

Turn

354 – 357

4

Beta strand

358 – 361

4

Helix

362 – 369

8

Sequences

	Sequence		Length	Mass (Da)
	P28623 [UniParc]. Last modified November 30, 2010. Version 2. Checksum: 57F15B035856008E	FASTA	515	55,978
	10 20 30 40 50 60 MIKHLLSRGK LLLFVSVMAT SSIIAGGNAY GSTAFTGVRD VPAQQIVNEM KVGWNLGNTM 70 80 90 100 110 120 DAIGGETNWG NPMTTHAMIN KIKEAGFNTL RLPVTWDGHM GAAPEYTIDQ TWMKRVEEIA 130 140 150 160 170 180 NYAFDNDMYV IINLHHENEW LKPFYANEAQ VKAQLTKVWT QIANNFKKYG DHLIFETMNE 190 200 210 220 230 240 PRPVGASNEW TGGSYENREV VNRYNLTAVN AIRATGGNNA TRYIMVPTLA ASAMSTTIND 250 260 270 280 290 300 LVIPNNDSKV IVSLHMYSPY FFAMDINGTS SWGSDYDKSS LDSEFDAVYN KFVKNGRAVV 310 320 330 340 350 360 IGEMGSINKN NTAARVTHAE YYAKSAKARG LTPIWWDNGY SVAGKAETFG IFNRSNLTWD 370 380 390 400 410 420 APEVMKAFIK GIGGSSTTTP TTPTTPTTPT TPTTPTTPTT PTTPTTPQSA VEVTYAITNS 430 440 450 460 470 480 WGSGASVNVT IKNNGTTPIN GWTLKWTMPI NQTITNMWSA SFVASGTTLS VTNAGYNGTI 490 500 510 AANGGTQSFG FNINYSGVLS KPTGFTVNGT ECTVK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of functional domains of endoglucanases from Clostridium cellulovorans by gene cloning, nucleotide sequencing and chimeric protein construction." Hamamoto T., Foong F., Shoseyov O., Doi R.H. Mol. Gen. Genet. 231:472-479(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 32-44.
[2]	"Complete sequence of Clostridium cellulovorans 743B." US DOE Joint Genome Institute Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., Hemme C.L., Woyke T. Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35296 / DSM 3052 / OCM 3 / 743B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M37434 Genomic DNA. Translation: AAA23233.1.
CP002160 Genomic DNA. Translation: ADL52928.1.

PIR

S20493.

RefSeq

YP_003844692.1. NC_014393.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3NDY	X-ray	2.10	A/B/C/D	32-376	[»]
			E/F/G/H	409-515	[»]
3NDZ	X-ray	2.08	A/B/C/D	32-376	[»]
			E/F/G/H	409-515	[»]

ProteinModelPortal

P28623.

ModBase

Search...

Protein family/group databases

CAZy

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

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

ADL52928; ADL52928; Clocel_3242.

GeneID

9610136.

KEGG

ccb:Clocel_3242.

PATRIC

41732687. VBICloCel81632203721_0262.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

HOG000027405.

Enzyme and pathway databases

BioCyc

CCEL573061:GIXD-3329-MONOMER.

Family and domain databases

Gene3D

2.60.40.290. 1 hit.
3.20.20.80. 1 hit.

InterPro

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]

Pfam

PF00553. CBM_2. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]

SMART

SM00637. CBD_II. 1 hit.
[Graphical view]

SUPFAM

SSF49384. Cellul_bind. 1 hit.
SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS51173. CBM2. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P28623.

Entry information

Entry name

GUND_CLOC7

Accession

Primary (citable) accession number: P28623
Secondary accession number(s): D9SUH3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	November 30, 2010
Last modified:	May 1, 2013
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program