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Q8L5J1

- MAN4_SOLLC

UniProt

Q8L5J1 - MAN4_SOLLC

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Protein

Mannan endo-1,4-beta-mannosidase 4

Gene
MAN4
Organism
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Possesses endo-beta-mannanase and mannan transglycosylase activities. May be involved in cell wall degradation during fruit ripening.2 Publications

Catalytic activityi

Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.

pH dependencei

Optimum pH is 5.0 for both endo-beta-mannanase and mannan transglycosylase activities.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei204 – 2041Proton donor By similarity
Active sitei318 – 3181Nucleophile By similarity

GO - Molecular functioni

  1. mannan endo-1,4-beta-mannosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
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 namesi
Name:MAN4
OrganismiSolanum lycopersicum (Tomato) (Lycopersicon esculentum)
Taxonomic identifieri4081 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumLycopersicon
ProteomesiUP000004994: Chromosome 1

Subcellular locationi

Secreted Reviewed prediction

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi394 – 3996RLSKLS → ALS: Activity reduced by 5-fold. 1 Publication
Mutagenesisi394 – 3941R → A: Activity slightly reduced.
Mutagenesisi396 – 3994Missing: Activity reduced by 8-fold.
Mutagenesisi397 – 3993Missing: Activity reduced by 3-fold.
Mutagenesisi398 – 3992Missing: Activity reduced by 5-fold.
Mutagenesisi399 – 3991Missing: No effect on activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26262 PublicationsAdd
BLAST
Chaini27 – 399373Mannan endo-1,4-beta-mannosidase 4PRO_0000277492Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi347 ↔ 3541 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed in flowers and fruit pericarp.1 Publication

Structurei

Secondary structure

1
399
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 363
Beta strandi39 – 424
Beta strandi45 – 473
Beta strandi49 – 535
Helixi57 – 626
Turni64 – 674
Helixi68 – 7912
Beta strandi84 – 907
Beta strandi92 – 965
Beta strandi98 – 1014
Helixi107 – 12216
Beta strandi126 – 1305
Beta strandi133 – 1408
Helixi141 – 15010
Helixi158 – 1625
Helixi165 – 18016
Turni184 – 1863
Helixi190 – 1923
Beta strandi196 – 2016
Helixi214 – 23017
Beta strandi233 – 2375
Helixi246 – 2516
Helixi253 – 2553
Helixi262 – 2665
Beta strandi274 – 2774
Helixi280 – 2834
Helixi289 – 31022
Beta strandi314 – 3185
Helixi330 – 34920
Beta strandi353 – 3608
Helixi368 – 3703
Helixi378 – 3803
Helixi382 – 39514

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RH9X-ray1.50A27-399[»]
ProteinModelPortaliQ8L5J1.
SMRiQ8L5J1. Positions 30-399.

Miscellaneous databases

EvolutionaryTraceiQ8L5J1.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

OMAiLWITSHA.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8L5J1-1 [UniParc]FASTAAdd to Basket

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MNNSIILIFV AILIIFPNEF SKPTRAFSNN NFVYTDGTHF ALNGKSLYIN    50
GFNAYWLMYI AYDPSTRIKV TNTFQQASKY KMNVARTWAF SHGGSRPLQS 100
APGVYNEQMF QGLDFVISEA KKYGIHLIMS LVNNWDAFGG KKQYVEWAVQ 150
RGQKLTSDDD FFTNPMVKGF YKNNVKVVLT RVNTITKVAY KDDPTILSWE 200
LINEPRCPSD LSGKTFQNWV LEMAGYLKSI DSNHLLEIGL EGFYGNDMRQ 250
YNPNSYIFGT NFISNNQVQG IDFTTIHMYP NQWLPGLTQE AQDKWASQWI 300
QVHIDDSKML KKPLLIAEFG KSTKTPGYTV AKRDNYFEKI YGTIFNCAKS 350
GGPCGGGLFW QVLGQGMSSF DDGYQVVLQE SPSTSRVILL QSLRLSKLS 399
Length:399
Mass (Da):45,339
Last modified:February 6, 2007 - v2
Checksum:i805A7D7866E5FF6B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti394 – 3996RLSKLS → AL in strain: cv. Castalia and cv. Walter; in allele LeMAN4i; inactive enzyme.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti274 – 2741T → A in AAK56557. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY046588 mRNA. Translation: AAK97760.1.
AY046589 mRNA. Translation: AAK97759.2.
AY034075 mRNA. Translation: AAK56557.1.
RefSeqiNP_001234114.1. NM_001247185.1.
NP_001234131.1. NM_001247202.1.
NP_001234874.1. NM_001247945.1.
UniGeneiLes.22467.
Les.25883.
Les.25913.

Genome annotation databases

EnsemblPlantsiSolyc01g008710.2.1; Solyc01g008710.2.1; Solyc01g008710.2.
GeneIDi543823.
543828.
544253.
KEGGisly:543823.
sly:543828.
sly:544253.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY046588 mRNA. Translation: AAK97760.1 .
AY046589 mRNA. Translation: AAK97759.2 .
AY034075 mRNA. Translation: AAK56557.1 .
RefSeqi NP_001234114.1. NM_001247185.1.
NP_001234131.1. NM_001247202.1.
NP_001234874.1. NM_001247945.1.
UniGenei Les.22467.
Les.25883.
Les.25913.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1RH9 X-ray 1.50 A 27-399 [» ]
ProteinModelPortali Q8L5J1.
SMRi Q8L5J1. Positions 30-399.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi Solyc01g008710.2.1 ; Solyc01g008710.2.1 ; Solyc01g008710.2 .
GeneIDi 543823.
543828.
544253.
KEGGi sly:543823.
sly:543828.
sly:544253.

Phylogenomic databases

OMAi LWITSHA.

Miscellaneous databases

EvolutionaryTracei Q8L5J1.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00150. Cellulase. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiMAN4_SOLLC
AccessioniPrimary (citable) accession number: Q8L5J1
Secondary accession number(s): Q8RVL3, Q93WT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: February 6, 2007
Last modified: May 14, 2014
This is version 58 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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