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Q8WPJ2

- MANA_MYTED

UniProt

Q8WPJ2 - MANA_MYTED

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Protein
Mannan endo-1,4-beta-mannosidase
Gene
N/A
Organism
Mytilus edulis (Blue mussel)
Status
Reviewed - 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 mannopentaose
  3. KM=0.5 mM for mannohexaose

pH dependencei

Optimum pH is 5.2.

Temperature dependencei

Optimum temperature is about 50 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei177 – 1771Proton donor By similarityBy similarity
Active sitei308 – 3081Nucleophile By similarityBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. mannan catabolic process Source: UniProtKB
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 (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)
Taxonomic identifieri6550 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaBivalviaPteriomorphiaMytiloidaMytiloideaMytilidaeMytilinaeMytilus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17171 Publication
Add
BLAST
Chaini18 – 367350Mannan endo-1,4-beta-mannosidase1 Publication
PRO_0000007901Add
BLAST

Amino acid modifications

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

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C0HX-ray1.60A15-367[»]
ProteinModelPortaliQ8WPJ2.
SMRiQ8WPJ2. Positions 18-367.

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

MLLTALAVLF ASTGCQARLS VSGTNLNYNG HHIFLSGANQ AWVNYARDFG    50
HNQYSKGKST FESTLSDIQS HGGNSVRVWL HIEGESTPEF DNNGYVTGID 100
NTLISDMRAY LHAAQRHNIL IFFTLWNGAV KQSTHYRLNG LMVDTRKLQS 150
YIDHALKPMA NALKNEKALG GWDIMNEPEG EIKPGESSSE PCFDTRHLSG 200
SGAGWAGHLY SAQEIGRFVN WQAAAIKEVD PGAMVTVGSW NMKADTDAMG 250
FHNLYSDHCL VKAGGKQSGT LSFYQVHTYD WQNHFGNESP FKHSFSNFRL 300
KKPMVIGEFN QEHGAGMSSE SMFEWAYTKG YSGAWTWSRT DVSWNNQLRG 350
IQHLKSRTDH GQVQFGL 367
Length:367
Mass (Da):40,957
Last modified:March 1, 2002 - v1
Checksum:iB364E03418D2EA86
GO

Mass spectrometryi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681I → M no nucleotide entry 1 Publication
Sequence conflicti351 – 3511I → M no nucleotide entry 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ271365 Genomic DNA. Translation: CAC81056.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ271365 Genomic DNA. Translation: CAC81056.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2C0H X-ray 1.60 A 15-367 [» ]
ProteinModelPortali Q8WPJ2.
SMRi Q8WPJ2. Positions 18-367.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q8WPJ2.

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. "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 gland and Gill.
  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 gland.
  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: July 9, 2014
This is version 61 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