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P49424 (MANA_CELJU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mannan endo-1,4-beta-mannosidase
EC=3.2.1.78
Alternative name(s):
Mannanase A
Gene names
Name:manA
Synonyms:man26A
Ordered Locus Names:CJA_2770
OrganismCellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa) [Complete proteome] [HAMAP]
Taxonomic identifier498211 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Cellvibrio ›

Protein attributes

Sequence length423 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes mannan and galactomannan, but displays little activity towards other polysaccharides located in the plant cell wall. Appears to act in synergy with alpha-galactosidase (AgaA) to elicit hydrolysis of galactomannan. Preferentially hydrolyzes the larger oligosaccharides and has greater activity against non-substituted polysaccharides. Ref.1 Ref.4

Catalytic activity

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

Sequence similarities

Belongs to the glycosyl hydrolase 26 family.

Biophysicochemical properties

pH dependence:

Optimum pH is about 7.0.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Propeptide32 – 387 Potential
PRO_0000012172
Chain39 – 423385Mannan endo-1,4-beta-mannosidase
PRO_0000012173

Secondary structure

1 ..................................................................... 423
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P49424 [UniParc].

Last modified July 5, 2005. Version 2.
Checksum: EFDAB597F10BA3DD

FASTA42347,487
        10         20         30         40         50         60 
MKTITTARLP WAAQSFALGI CLIALLGCNH AANKSSASRA DVKPVTVKLV DSQATMETRS 

        70         80         90        100        110        120 
LFAFMQEQRR HSIMFGHQHE TTQGLTITRT DGTQSDTFNA VGDFAAVYGW DTLSIVAPKA 

       130        140        150        160        170        180 
EGDIVAQVKK AYARGGIITV SSHFDNPKTD TQKGVWPVGT SWDQTPAVVD SLPGGAYNPV 

       190        200        210        220        230        240 
LNGYLDQVAE WANNLKDEQG RLIPVIFRLY HENTGSWFWW GDKQSTPEQY KQLFRYSVEY 

       250        260        270        280        290        300 
LRDVKGVRNF LYAYSPNNFW DVTEANYLER YPGDEWVDVL GFDTYGPVAD NADWFRNVVA 

       310        320        330        340        350        360 
NAALVARMAE ARGKIPVISE IGIRAPDIEA GLYDNQWYRK LISGLKADPD AREIAFLLVW 

       370        380        390        400        410        420 
RNAPQGVPGP NGTQVPHYWV PANRPENINN GTLEDFQAFY ADEFTAFNRD IEQVYQRPTL 


IVK

« Hide

References

« Hide 'large scale' references
[1]"A non-modular endo-beta-1,4-mannanase from Pseudomonas fluorescens subspecies cellulosa."
Braithwaite K.L., Black G.W., Hazlewood G.P., Ali B.R.S., Gilbert H.J.
Biochem. J. 305:1005-1010(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 39-48, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, PH DEPENDENCE.
[2]Gilbert H.J.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 364-423.
[3]"Insights into plant cell wall degradation from the genome sequence of the soil bacterium Cellvibrio japonicus."
DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H., Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J., Nelson K.E.
J. Bacteriol. 190:5455-5463(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ueda107.
[4]"alpha-Galactosidase A from Pseudomonas fluorescens subsp. cellulosa: cloning, high level expression and its role in galactomannan hydrolysis."
Halstead J.R., Fransen M.P., Eberhart R.Y., Park A.J., Gilbert H.J., Hazlewood G.P.
FEMS Microbiol. Lett. 192:197-203(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X82179 Genomic DNA. Translation: CAA57670.2.
CP000934 Genomic DNA. Translation: ACE82849.1.
PIRS53374.
RefSeqYP_001983229.1. NC_010995.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GVYX-ray1.70A39-421[»]
1GW1X-ray1.65A43-421[»]
1J9YX-ray1.85A39-423[»]
1ODZX-ray1.40A/B39-423[»]
1R7OX-ray1.85A29-423[»]
2WHMX-ray1.50A39-423[»]
ProteinModelPortalP49424.
SMRP49424. Positions 42-422.
ModBaseSearch...

Protein-protein interaction databases

STRING498211.CJA_2770.

Protein family/group databases

CAZyGH26. Glycoside Hydrolase Family 26.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACE82849; ACE82849; CJA_2770.
GeneID6414457.
KEGGcja:CJA_2770.
PATRIC21328934. VBICelJap122165_2735.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000274384.
OMAIANWANE.

Enzyme and pathway databases

BioCycCJAP498211:GHIT-227-MONOMER.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR022790. EndoGluc_H/Glyco_hydro_26.
IPR000805. Glyco_hydro_26.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF02156. Glyco_hydro_26. 1 hit.
[Graphical view]
PRINTSPR00739. GLHYDRLASE26.
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP49424.

Entry information

Entry nameMANA_CELJU
AccessionPrimary (citable) accession number: P49424
Secondary accession number(s): B3PBK3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: July 5, 2005
Last modified: May 1, 2013
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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