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Q8L5J1

- MAN4_SOLLC

UniProt

Q8L5J1 - MAN4_SOLLC

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
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 2 (06 Feb 2007)
      Previous versions | rss
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    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 donorBy similarity
    Active sitei318 – 3181NucleophileBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    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 Curated

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    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. 1 Publication
    Mutagenesisi396 – 3994Missing: Activity reduced by 8-fold. 1 Publication
    Mutagenesisi397 – 3993Missing: Activity reduced by 3-fold. 1 Publication
    Mutagenesisi398 – 3992Missing: Activity reduced by 5-fold. 1 Publication
    Mutagenesisi399 – 3991Missing: No effect on activity. 1 Publication

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    « Hide

    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

    Experimental Info

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

    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 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: October 1, 2014
    This is version 59 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