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Q8L5J1 (MAN4_SOLLC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSolanum lycopersicum (Tomato) (Lycopersicon esculentum) [Reference proteome]
Taxonomic identifier4081 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumLycopersicon

Protein attributes

Sequence length399 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Ref.3

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmannan endo-1,4-beta-mannosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.1 Ref.3
Chain27 – 399373Mannan endo-1,4-beta-mannosidase 4
PRO_0000277492

Sites

Active site2041Proton donor By similarity
Active site3181Nucleophile By similarity

Amino acid modifications

Disulfide bond347 ↔ 354 Ref.4

Natural variations

Natural variant394 – 3996RLSKLS → AL in strain: cv. Castalia and cv. Walter; in allele LeMAN4i; inactive enzyme.

Experimental info

Mutagenesis394 – 3996RLSKLS → ALS: Activity reduced by 5-fold. Ref.1
Mutagenesis3941R → A: Activity slightly reduced.
Mutagenesis396 – 3994Missing: Activity reduced by 8-fold.
Mutagenesis397 – 3993Missing: Activity reduced by 3-fold.
Mutagenesis398 – 3992Missing: Activity reduced by 5-fold.
Mutagenesis3991Missing: No effect on activity.
Sequence conflict2741T → A in AAK56557. Ref.2

Secondary structure

................................................................. 399
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8L5J1 [UniParc].

Last modified February 6, 2007. Version 2.
Checksum: 805A7D7866E5FF6B

FASTA39945,339
        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 

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 27-399, DISULFIDE BOND.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY046588 mRNA. Translation: AAK97760.1.
AY046589 mRNA. Translation: AAK97759.2.
AY034075 mRNA. Translation: AAK56557.1.
RefSeqNP_001234114.1. NM_001247185.1.
NP_001234131.1. NM_001247202.1.
NP_001234874.1. NM_001247945.1.
UniGeneLes.22467.
Les.25883.
Les.25913.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RH9X-ray1.50A27-399[»]
ProteinModelPortalQ8L5J1.
SMRQ8L5J1. Positions 30-399.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsSolyc01g008710.2.1; Solyc01g008710.2.1; Solyc01g008710.2.
GeneID543823.
543828.
544253.
KEGGsly:543823.
sly:543828.
sly:544253.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ8L5J1.

Entry information

Entry nameMAN4_SOLLC
AccessionPrimary (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: February 19, 2014
This is version 57 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries