Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8WPJ2

- MANA_MYTED

UniProt

Q8WPJ2 - MANA_MYTED

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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 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

  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)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
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 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: November 26, 2014
This is version 63 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