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Protein

Mannan endo-1,4-beta-mannosidase

Gene
N/A
Organism
Mytilus edulis (Blue mussel)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes 1,4-beta linked polysaccharide backbones of mannans. Hydrolyzes mannohexaose (M6) preferentially to mannotriose (M4) and less preferentially to mannotetraose (M3), mannopentaose (M5), and mannobiose (M2); hydrolyzes M5 preferentially to M2, and M3, and less preferentially to mannotetraose M4; hydrolyzes M4 preferentially to M3, and less preferentially to mannose (M1), plus very little M2. Does not hydrolyze mannobiose or mannotriose. Does not hydrolyze xlyan, starch, cellulose or galactose.3 Publications

Catalytic activityi

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

Kineticsi

  1. KM=2.49 mM for mannotetraose2 Publications
  2. KM=1.61 mM for mannopentaose2 Publications
  3. KM=0.5 mM for mannohexaose2 Publications

    pH dependencei

    Optimum pH is 5.2.2 Publications

    Temperature dependencei

    Optimum temperature is about 50 degrees Celsius.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei177 – 1771Proton donorBy similarity
    Active sitei308 – 3081NucleophileBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    • mannan catabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BRENDAi3.2.1.78. 3544.

    Protein family/group databases

    CAZyiGH5. Glycoside Hydrolase Family 5.

    Names & Taxonomyi

    Protein namesi
    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:
    Man5A
    Short name:
    ManA
    OrganismiMytilus edulis (Blue mussel)Imported
    Taxonomic identifieri6550 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaBivalviaPteriomorphiaMytiloidaMytiloideaMytilidaeMytilinaeMytilus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 17171 PublicationAdd
    BLAST
    Chaini18 – 367350Mannan endo-1,4-beta-mannosidase1 PublicationPRO_0000007901Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi192 ↔ 259Curated

    Post-translational modificationi

    The disulfide bond between Cys-192 and Cys-259 has not been observed in x-ray crystallograghy (PubMed:16487541). This may be a consequence of the X-ray radiation.1 Publication

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    Secondary structure

    1
    367
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi19 – 224Combined sources
    Beta strandi25 – 284Combined sources
    Beta strandi31 – 333Combined sources
    Beta strandi35 – 395Combined sources
    Beta strandi48 – 503Combined sources
    Helixi54 – 7017Combined sources
    Beta strandi75 – 828Combined sources
    Beta strandi84 – 907Combined sources
    Beta strandi96 – 983Combined sources
    Helixi103 – 11614Combined sources
    Beta strandi120 – 1278Combined sources
    Helixi135 – 1439Combined sources
    Helixi145 – 15410Combined sources
    Helixi156 – 1638Combined sources
    Beta strandi169 – 1768Combined sources
    Helixi178 – 1814Combined sources
    Helixi191 – 1933Combined sources
    Helixi196 – 1983Combined sources
    Turni203 – 2064Combined sources
    Helixi212 – 22918Combined sources
    Beta strandi235 – 2406Combined sources
    Helixi242 – 2443Combined sources
    Helixi257 – 2648Combined sources
    Beta strandi272 – 2776Combined sources
    Helixi295 – 2984Combined sources
    Beta strandi304 – 3085Combined sources
    Helixi311 – 3133Combined sources
    Helixi319 – 32810Combined sources
    Beta strandi332 – 3376Combined sources
    Beta strandi339 – 3424Combined sources
    Helixi344 – 35310Combined sources
    Turni354 – 3563Combined sources
    Beta strandi361 – 3644Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2C0HX-ray1.60A15-367[»]
    ProteinModelPortaliQ8WPJ2.
    SMRiQ8WPJ2. Positions 18-367.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8WPJ2.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    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.

    Q8WPJ2-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLLTALAVLF ASTGCQARLS VSGTNLNYNG HHIFLSGANQ AWVNYARDFG
    60 70 80 90 100
    HNQYSKGKST FESTLSDIQS HGGNSVRVWL HIEGESTPEF DNNGYVTGID
    110 120 130 140 150
    NTLISDMRAY LHAAQRHNIL IFFTLWNGAV KQSTHYRLNG LMVDTRKLQS
    160 170 180 190 200
    YIDHALKPMA NALKNEKALG GWDIMNEPEG EIKPGESSSE PCFDTRHLSG
    210 220 230 240 250
    SGAGWAGHLY SAQEIGRFVN WQAAAIKEVD PGAMVTVGSW NMKADTDAMG
    260 270 280 290 300
    FHNLYSDHCL VKAGGKQSGT LSFYQVHTYD WQNHFGNESP FKHSFSNFRL
    310 320 330 340 350
    KKPMVIGEFN QEHGAGMSSE SMFEWAYTKG YSGAWTWSRT DVSWNNQLRG
    360
    IQHLKSRTDH GQVQFGL
    Length:367
    Mass (Da):40,957
    Last modified:March 1, 2002 - v1
    Checksum:iB364E03418D2EA86
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti68 – 681I → M no nucleotide entry (PubMed:16487541).Curated
    Sequence conflicti351 – 3511I → M no nucleotide entry (PubMed:16487541).Curated

    Mass spectrometryi

    Molecular mass is 39702 Da from positions 18 - 367. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ271365 Genomic DNA. Translation: CAC81056.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ271365 Genomic DNA. Translation: CAC81056.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2C0HX-ray1.60A15-367[»]
    ProteinModelPortaliQ8WPJ2.
    SMRiQ8WPJ2. Positions 18-367.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiGH5. Glycoside Hydrolase Family 5.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BRENDAi3.2.1.78. 3544.

    Miscellaneous databases

    EvolutionaryTraceiQ8WPJ2.

    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.
    ProtoNetiSearch...

    Publicationsi

    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
      Tissue: Digestive gland1 Publication and Gill1 Publication.
    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] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 18-53, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY.
      Tissue: Digestive gland1 Publication.
    3. "Crystallization and X-ray analysis of native and selenomethionyl beta-mannanase Man5A from blue mussel, Mytilus edulis, expressed in Pichia pastoris."
      Xu B., Munoz I.G., Janson J.-C., Stahlberg J.
      Acta Crystallogr. D 58:542-545(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: CRYSTALLIZATION.
    4. "Three-dimensional crystal structure and enzymic characterization of beta-mannanase Man5A from blue mussel Mytilus edulis."
      Larsson A.M., Anderson L., Xu B., Munoz I.G., Uson I., Janson J.-C., Stalbrand H., Stahlberg J.
      J. Mol. Biol. 357:1500-1510(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 18-367, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiMANA_MYTED
    AccessioniPrimary (citable) accession number: Q8WPJ2
    Secondary accession number(s): P82544, P82801
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2004
    Last sequence update: March 1, 2002
    Last modified: April 1, 2015
    This is version 64 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.