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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)DescriptionActionsGraphical viewLength
    Active sitei177Proton donorBy similarity1
    Active sitei308NucleophileBy similarity1

    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)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 171 PublicationAdd BLAST17
    ChainiPRO_000000790118 – 367Mannan endo-1,4-beta-mannosidase1 PublicationAdd BLAST350

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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

    1367
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi19 – 22Combined sources4
    Beta strandi25 – 28Combined sources4
    Beta strandi31 – 33Combined sources3
    Beta strandi35 – 39Combined sources5
    Beta strandi48 – 50Combined sources3
    Helixi54 – 70Combined sources17
    Beta strandi75 – 82Combined sources8
    Beta strandi84 – 90Combined sources7
    Beta strandi96 – 98Combined sources3
    Helixi103 – 116Combined sources14
    Beta strandi120 – 127Combined sources8
    Helixi135 – 143Combined sources9
    Helixi145 – 154Combined sources10
    Helixi156 – 163Combined sources8
    Beta strandi169 – 176Combined sources8
    Helixi178 – 181Combined sources4
    Helixi191 – 193Combined sources3
    Helixi196 – 198Combined sources3
    Turni203 – 206Combined sources4
    Helixi212 – 229Combined sources18
    Beta strandi235 – 240Combined sources6
    Helixi242 – 244Combined sources3
    Helixi257 – 264Combined sources8
    Beta strandi272 – 277Combined sources6
    Helixi295 – 298Combined sources4
    Beta strandi304 – 308Combined sources5
    Helixi311 – 313Combined sources3
    Helixi319 – 328Combined sources10
    Beta strandi332 – 337Combined sources6
    Beta strandi339 – 342Combined sources4
    Helixi344 – 353Combined sources10
    Turni354 – 356Combined sources3
    Beta strandi361 – 364Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2C0HX-ray1.60A15-367[»]
    ProteinModelPortaliQ8WPJ2.
    SMRiQ8WPJ2.
    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)DescriptionActionsGraphical viewLength
    Sequence conflicti68I → M no nucleotide entry (PubMed:16487541).Curated1
    Sequence conflicti351I → M no nucleotide entry (PubMed:16487541).Curated1

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2C0HX-ray1.60A15-367[»]
    ProteinModelPortaliQ8WPJ2.
    SMRiQ8WPJ2.
    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...

    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: November 2, 2016
    This is version 68 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

    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 one 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.