Reviewed, UniProtKB/Swiss-Prot Q8L5J1 (MAN4_SOLLC)

Names and origin

Protein names

Recommended name:
    Mannan endo-1,4-beta-mannosidase 4
    EC=3.2.1.78
Alternative name(s):
    Beta-mannanase 4
    Endo-beta-1,4-mannanase 4
    LeMAN4a
    LeMAN4i

Gene names

Name:

MAN4

Organism

Solanum lycopersicum (Tomato) (Lycopersicon esculentum)

Taxonomic identifier

4081 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum › Lycopersicon

Protein attributes

Sequence length	399 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	Possesses endo-beta-mannanase and mannan transglycosylase activities. May be involved in cell wall degradation during fruit ripening. Ref.1 Ref.3
Catalytic activity	Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Subcellular location	Secreted Potential.
Tissue specificity	Expressed in flowers and fruit pericarp. Ref.2
Sequence similarities	Belongs to the glycosyl hydrolase 5 (cellulase A) family.
biophysicochemical properties	pH dependence: Optimum pH is 5.0 for both endo-beta-mannanase and mannan transglycosylase activities.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro mannan endo-1,4-beta-mannosidase 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 Ref.3

Chain

27 – 399

373

Mannan endo-1,4-beta-mannosidase 4

PRO_0000277492

Sites

Active site

204

1

Proton donor By similarity

Active site

318

1

Nucleophile By similarity

Amino acid modifications

Disulfide bond

347 ↔ 354

Ref.4

Natural variations

Natural variant

394 – 399

6

RLSKLS → AL in strain: cv. Castalia and cv. Walter; in allele LeMAN4i; inactive enzyme. Ref.1

Experimental info

Mutagenesis

394 – 399

6

RLSKLS → ALS: Activity reduced by 5-fold. Ref.1

Mutagenesis

394

1

R → A: Activity slightly reduced.

Mutagenesis

396 – 399

4

Missing: Activity reduced by 8-fold.

Mutagenesis

397 – 399

3

Missing: Activity reduced by 3-fold.

Mutagenesis

398 – 399

2

Missing: Activity reduced by 5-fold.

Mutagenesis

399

1

Missing: No effect on activity.

Sequence conflict

274

1

T → A in AAK56557. Ref.2

Secondary structure

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399

Helix Strand Turn

Details...

Beta strand

34 – 36

3

Beta strand

39 – 42

4

Beta strand

45 – 47

3

Beta strand

49 – 53

5

Helix

57 – 62

6

Turn

64 – 67

4

Helix

68 – 79

12

Beta strand

84 – 90

7

Beta strand

92 – 96

5

Beta strand

98 – 101

4

Helix

107 – 122

16

Beta strand

126 – 130

5

Beta strand

133 – 140

8

Helix

141 – 150

10

Helix

158 – 162

5

Helix

165 – 180

16

Turn

184 – 186

3

Helix

190 – 192

3

Beta strand

196 – 201

6

Helix

214 – 230

17

Beta strand

233 – 237

5

Helix

246 – 251

6

Helix

253 – 255

3

Helix

262 – 266

5

Beta strand

274 – 277

4

Helix

280 – 283

4

Helix

289 – 310

22

Beta strand

314 – 318

5

Helix

330 – 349

20

Beta strand

353 – 360

8

Helix

368 – 370

3

Helix

378 – 380

3

Helix

382 – 395

14

Sequences

	Sequence		Length	Mass (Da)
	Q8L5J1-1 [UniParc]. Last modified February 6, 2007. Version 2. Checksum: 805A7D7866E5FF6B	FASTA	399	45,339
	10 20 30 40 50 60 MNNSIILIFV AILIIFPNEF SKPTRAFSNN NFVYTDGTHF ALNGKSLYIN GFNAYWLMYI 70 80 90 100 110 120 AYDPSTRIKV TNTFQQASKY KMNVARTWAF SHGGSRPLQS APGVYNEQMF QGLDFVISEA 130 140 150 160 170 180 KKYGIHLIMS LVNNWDAFGG KKQYVEWAVQ RGQKLTSDDD FFTNPMVKGF YKNNVKVVLT 190 200 210 220 230 240 RVNTITKVAY KDDPTILSWE LINEPRCPSD LSGKTFQNWV LEMAGYLKSI DSNHLLEIGL 250 260 270 280 290 300 EGFYGNDMRQ YNPNSYIFGT NFISNNQVQG IDFTTIHMYP NQWLPGLTQE AQDKWASQWI 310 320 330 340 350 360 QVHIDDSKML KKPLLIAEFG KSTKTPGYTV AKRDNYFEKI YGTIFNCAKS GGPCGGGLFW 370 380 390 QVLGQGMSSF DDGYQVVLQE SPSTSRVILL QSLRLSKLS

References

[1]	"Variation in its C-terminal amino acids determines whether endo-beta-mannanase is active or inactive in ripening tomato fruits of different cultivars." Bourgault R., Bewley J.D. Plant Physiol. 130:1254-1262(2002) [PubMed: 12427992] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-39, FUNCTION, CHARACTERIZATION OF VARIANT 394-ARG--SER-399 DELINS ALA-LEU, MUTAGENESIS OF 394-ARG--SER-399. Strain: cv. Trust and cv. Walter. Tissue: Pericarp.
[2]	"Characterisation of an endo-(1,4)-beta-mannanase expressed in ripening tomato fruit." Carrington C.M.S., Vendrell M., Dominguez-Puigjaner E. Plant Sci. 163:599-606(2002) Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: cv. Castalia. Tissue: Pericarp.
[3]	"LeMAN4 endo-beta-mannanase from ripe tomato fruit can act as a mannan transglycosylase or hydrolase." Schroeder R., Wegrzyn T.F., Sharma N.N., Atkinson R.G. Planta 224:1091-1102(2006) [PubMed: 16649044] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-56, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[4]	"Three-dimensional structure of (1,4)-beta-D-mannan mannanohydrolase from tomato fruit." Bourgault R., Oakley A.J., Bewley J.D., Wilce M.C.J. Protein Sci. 14:1233-1241(2005) [PubMed: 15840830] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 27-399, DISULFIDE BOND.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AY046588 mRNA. Translation: AAK97760.1.
AY046589 mRNA. Translation: AAK97759.2.
AY034075 mRNA. Translation: AAK56557.1.

UniGene

Les.22363
Les.22397
Les.268

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RH9	X-ray	1.50	A	27-399	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH5. Glycoside Hydrolase Family 5.

Family and domain databases

InterPro

IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

PROSITE

PS00659. GLYCOSYL_HYDROL_F5. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

MAN4_SOLLC

Accession

Primary (citable) accession number: Q8L5J1
Secondary accession number(s): Q8RVL3, Q93WT4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 6, 2007
Last sequence update:	February 6, 2007
Last modified:	June 16, 2009
This is version 39 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)