O85465 (GUN5_BACAG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endoglucanase 5A
EC=3.2.1.4

Alternative name(s):
Alkaline cellulase
Endo-1,4-beta-glucanase 5A

Gene names

Name:

cel5A

Organism

Bacillus agaradhaerens (Bacillus agaradherans)

Taxonomic identifier

76935 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	400 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Subunit structure	Monomer.
Sequence similarities	Belongs to the glycosyl hydrolase 5 (cellulase A) family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: InterPro
Molecular_function	carbohydrate 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

Chain

1 – 400

400

Endoglucanase 5A

PRO_0000184043

Sites

Active site

165

1

Proton donor

Active site

254

1

Nucleophile

Secondary structure

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400

Helix Strand Turn

Details...

Helix

31 – 35

5

Beta strand

39 – 41

3

Beta strand

44 – 46

3

Beta strand

56 – 61

6

Helix

63 – 66

4

Helix

67 – 69

3

Helix

72 – 80

9

Beta strand

86 – 94

9

Turn

98 – 100

3

Helix

104 – 118

15

Beta strand

121 – 127

7

Beta strand

129 – 131

3

Turn

134 – 137

4

Helix

138 – 152

15

Beta strand

158 – 161

4

Turn

173 – 176

4

Helix

177 – 189

13

Beta strand

193 – 195

3

Beta strand

197 – 199

3

Helix

202 – 205

4

Helix

208 – 212

5

Beta strand

221 – 228

8

Turn

229 – 231

3

Helix

234 – 245

12

Beta strand

250 – 258

9

Beta strand

264 – 266

3

Helix

268 – 280

13

Beta strand

285 – 291

7

Helix

312 – 314

3

Helix

317 – 328

12

Sequences

	Sequence		Length	Mass (Da)
	O85465 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 3F9C66FB9BC36FFF	FASTA	400	44,702
	10 20 30 40 50 60 MKKITTIFVV LLMTVALFSI GNTTAADNDS VVEEHGQLSI SNGELVNERG EQVQLKGMSS 70 80 90 100 110 120 HGLQWYGQFV NYESMKWLRD DWGINVFRAA MYTSSGGYID DPSVKEKVKE AVEAAIDLDI 130 140 150 160 170 180 YVIIDWHILS DNDPNIYKEE AKDFFDEMSE LYGDYPNVIY EIANEPNGSD VTWGNQIKPY 190 200 210 220 230 240 AEEVIPIIRN NDPNNIIIVG TGTWSQDVHH AADNQLADPN VMYAFHFYAG THGQNLRDQV 250 260 270 280 290 300 DYALDQGAAI FVSEWGTSAA TGDGGVFLDE AQVWIDFMDE RNLSWANWSL THKDESSAAL 310 320 330 340 350 360 MPGANPTGGW TEAELSPSGT FVREKIRESA SIPPSDPTPP SDPGEPDPTP PSDPGEYPAW 370 380 390 400 DPNQIYTNEI VYHNGQLWQA KWWTQNQEPG DPYGPWEPLN

References

[1]	Bjornvad M.E. Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 700163 / DSM 8721 / LMG 17948 / NCIMB 40482.
[2]	"Structure of the Bacillus agaradherans family 5 endoglucanase at 1.6-A and its cellobiose complex at 2.0-A resolution." Davies G.J., Dauter M., Brzozowski A.M., Bjoernvad M.E., Andersen K.V., Schuelein M. Biochemistry 37:1926-1932(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 30-329. Strain: ATCC 700163 / DSM 8721 / LMG 17948 / NCIMB 40482.
[3]	"Snapshots along an enzymatic reaction coordinate: analysis of a retaining beta-glycoside hydrolase." Davies G.J., MacKenzie L.F., Varrot A., Dauter M., Brzozowski A.M., Schuelein M., Withers S.G. Biochemistry 37:11707-11713(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 30-329. Strain: ATCC 700163 / DSM 8721 / LMG 17948 / NCIMB 40482.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF067428 Genomic DNA. Translation: AAC19169.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A3H	X-ray	1.57	A	30-329	[»]
1E5J	X-ray	1.85	A	27-331	[»]
1H11	X-ray	1.08	A	27-329	[»]
1H2J	X-ray	1.15	A	27-329	[»]
1H5V	X-ray	1.10	A	30-330	[»]
1HF6	X-ray	1.15	A	27-329	[»]
1OCQ	X-ray	1.08	A	27-329	[»]
1QHZ	X-ray	1.95	A	27-331	[»]
1QI0	X-ray	2.10	A	27-331	[»]
1QI2	X-ray	1.75	A	27-331	[»]
1W3K	X-ray	1.20	A	27-329	[»]
1W3L	X-ray	1.04	A	27-329	[»]
2A3H	X-ray	2.00	A	30-329	[»]
2V38	X-ray	1.50	A	27-331	[»]
3A3H	X-ray	1.64	A	30-329	[»]
4A3H	X-ray	1.65	A	27-329	[»]
5A3H	X-ray	1.82	A	27-329	[»]
6A3H	X-ray	1.68	A	27-329	[»]
7A3H	X-ray	0.95	A	27-329	[»]
8A3H	X-ray	0.97	A	27-329	[»]

ProteinModelPortal

O85465.

SMR

O85465. Positions 30-331.

ModBase

Search...

Protein family/group databases

CAZy

CBM5. Carbohydrate-Binding Module Family 5.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

2.10.10.20. 1 hit.
3.20.20.80. 1 hit.

InterPro

IPR003610. CBM_fam5/12.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Pfam

PF02839. CBM_5_12. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]

SMART

SM00495. ChtBD3. 1 hit.
[Graphical view]

SUPFAM

SSF51055. CBM_5_12. 1 hit.
SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O85465.

Entry information

Entry name

GUN5_BACAG

Accession

Primary (citable) accession number: O85465

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	November 1, 1998
Last modified:	May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program