Reviewed, UniProtKB/Swiss-Prot Q8WPJ2 (MANA_MYTED)

Names and origin

Protein names	Recommended name:     Mannan endo-1,4-beta-mannosidase     EC=3.2.1.78 Alternative name(s):     Beta-mannanase     Endo-beta-1,4-mannanase       Short name=ManA
Organism	Mytilus edulis (Blue mussel)
Taxonomic identifier	6550 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Mollusca › Bivalvia › Pteriomorphia › Mytiloida › Mytiloidea › Mytilidae › Mytilinae › Mytilus

Protein attributes

Sequence length	367 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	Hydrolyzes 1,4-beta linked polysaccharide backbones of mannans. Hydrolyzes mannopentaose mainly to mannobiose, mannotriose and mannotetraose, and mannotetraose to mannose and mannotriose plus very little mannobiose. Does not hydrolyze mannobiose or mannotriose. Does not hydrolyze xlyan, starch, cellulose or galactose. Ref.1 Ref.2
Catalytic activity	Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Subunit structure	Monomer. Ref.2
Sequence similarities	Belongs to the glycosyl hydrolase 5 (cellulase A) family.
Biophysicochemical properties	pH dependence: Optimum pH is 5.2. Temperature dependence: Optimum temperature is about 50 degrees Celsius.
Mass spectrometry	Molecular mass is 39702 Da from positions 18 - 367. Determined by MALDI. Ref.2

Ontologies

Keywords
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	mannan catabolic process Ref.2 Inferred from direct assay. Source: UniProtKB
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro mannan endo-1,4-beta-mannosidase activity Ref.2 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Ref.2

Chain

18 – 367

350

Mannan endo-1,4-beta-mannosidase Ref.2

PRO_0000007901

Sites

Active site

177

1

Proton donor By similarity UniProtKB P07985

Active site

308

1

Nucleophile By similarity UniProtKB P07985

Secondary structure

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367

Helix Strand Turn

Details...

Beta strand

19 – 22

4

Beta strand

25 – 28

4

Beta strand

31 – 33

3

Beta strand

35 – 39

5

Beta strand

48 – 50

3

Helix

54 – 70

17

Beta strand

75 – 82

8

Beta strand

84 – 90

7

Beta strand

96 – 98

3

Helix

103 – 116

14

Beta strand

120 – 127

8

Helix

135 – 143

9

Helix

145 – 154

10

Helix

156 – 163

8

Beta strand

169 – 176

8

Helix

178 – 181

4

Helix

191 – 193

3

Helix

196 – 198

3

Turn

203 – 206

4

Helix

212 – 229

18

Beta strand

235 – 240

6

Helix

242 – 244

3

Helix

257 – 264

8

Beta strand

272 – 277

6

Helix

295 – 298

4

Beta strand

304 – 308

5

Helix

311 – 313

3

Helix

319 – 328

10

Beta strand

332 – 337

6

Beta strand

339 – 342

4

Helix

344 – 353

10

Turn

354 – 356

3

Beta strand

361 – 364

4

Sequences

	Sequence		Length	Mass (Da)
	Q8WPJ2-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: B364E03418D2EA86	FASTA	367	40,957
	10 20 30 40 50 60 MLLTALAVLF ASTGCQARLS VSGTNLNYNG HHIFLSGANQ AWVNYARDFG HNQYSKGKST 70 80 90 100 110 120 FESTLSDIQS HGGNSVRVWL HIEGESTPEF DNNGYVTGID NTLISDMRAY LHAAQRHNIL 130 140 150 160 170 180 IFFTLWNGAV KQSTHYRLNG LMVDTRKLQS YIDHALKPMA NALKNEKALG GWDIMNEPEG 190 200 210 220 230 240 EIKPGESSSE PCFDTRHLSG SGAGWAGHLY SAQEIGRFVN WQAAAIKEVD PGAMVTVGSW 250 260 270 280 290 300 NMKADTDAMG FHNLYSDHCL VKAGGKQSGT LSFYQVHTYD WQNHFGNESP FKHSFSNFRL 310 320 330 340 350 360 KKPMVIGEFN QEHGAGMSSE SMFEWAYTKG YSGAWTWSRT DVSWNNQLRG IQHLKSRTDH GQVQFGL

References

[1]	"Cloning and expression in Pichia pastoris of a blue mussel (Mytilus edulis) beta-mannanase gene." Xu B., Sellos D., Janson J.-C. Eur. J. Biochem. 269:1753-1760(2002) [PubMed: 11895446] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Tissue: Digestive gland and Gill.
[2]	"endo-beta-1,4-mannanases from blue mussel, Mytilus edulis: purification, characterization, and mode of action." Xu B., Hagglund P., Stalbrand H., Janson J.-C. J. Biotechnol. 92:267-277(2002) [PubMed: 11689251] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-53, FUNCTION, SUBUNIT, MASS SPECTROMETRY. Tissue: Digestive gland.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ271365 Genomic DNA. Translation: CAC81056.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2C0H	X-ray	1.60	A	18-367	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH5. Glycoside Hydrolase Family 5.

Enzyme and pathway databases

BRENDA

3.2.1.78. 8413.

Family and domain databases

InterPro

IPR001547. Glyco_hydro_5.
IPR017853. Glyco_hydro_catalytic_core.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

Pfam

PF00150. Cellulase. 1 hit.
[Graphical view]

PROSITE

PS00659. GLYCOSYL_HYDROL_F5. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

MANA_MYTED

Accession

Primary (citable) accession number: Q8WPJ2
Secondary accession number(s): P82544, P82801

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2004
Last sequence update:	March 1, 2002
Last modified:	January 19, 2010
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)