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P48841 (GANA_CELJU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Arabinogalactan endo-1,4-beta-galactosidase
EC=3.2.1.89
Alternative name(s):
Endo-1,4-beta-galactanase
Short name=Galactanase
Gene names
Name:ganB
Synonyms:gal53A-2, galA, ganA
Ordered Locus Names:CJA_0497
OrganismCellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa) [Complete proteome] [HAMAP]
Taxonomic identifier498211 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Cellvibrio

Protein attributes

Sequence length376 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-beta-D-galactosidic linkages in arabinogalactans.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Induction

By galactan. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 53 family.

Biophysicochemical properties

Kinetic parameters:

KM=2.3 mM for 2,4-dinitrophenyl-beta-galactobioside (at pH 7 and 37 degrees Celsius) Ref.1

pH dependence:

Optimum pH is 7.5.

Temperature dependence:

Optimum temperature is 60 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 376359Arabinogalactan endo-1,4-beta-galactosidase
PRO_0000012220

Sites

Active site1611Proton donor
Active site2701Nucleophile
Metal binding2811Calcium By similarity
Metal binding2851Calcium By similarity

Experimental info

Mutagenesis1611E → A: Partial loss of activity. Ref.1
Mutagenesis2701E → A: Complete loss of activity. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P48841 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: BEC4F7243C6CAE10

FASTA37642,315
        10         20         30         40         50         60 
MKKKILAATA ILLAAIANTG VADNTPFYVG ADLSYVNEME SCGATYRDQG KKVDPFQLFA 

        70         80         90        100        110        120 
DKGADLVRVR LWHNATWTKY SDLKDVSKTL KRAKNAGMKT LLDFHYSDTW TDPEKQFIPK 

       130        140        150        160        170        180 
AWAHITDTKE LAKALYDYTT DTLASLDQQQ LLPNLVQVGN ETNIEILQAE DTLVHGIPNW 

       190        200        210        220        230        240 
QRNATLLNSG VNAVRDYSKK TGKPIQVVLH IAQPENALWW FKQAKENGVI DYDVIGLSYY 

       250        260        270        280        290        300 
PQWSEYSLPQ LPDAIAELQN TYHKPVMIVE TAYPWTLHNF DQAGNVLGEK AVQPEFPASP 

       310        320        330        340        350        360 
RGQLTYLLTL TQLVKSAGGM GVIYWEPAWV STRCRTLWGK GSHWENASFF DATRKNNALP 

       370 
AFLFFKADYQ ASAQAE

« Hide

References

« Hide 'large scale' references
[1]"Evidence that galactanase A from Pseudomonas fluorescens subspecies cellulosa is a retaining family 53 glycosyl hydrolase in which E161 and E270 are the catalytic residues."
Braithwaite K.L., Barna T., Spurway T.D., Charnock S.J., Black G.W., Hughes N., Lakey J.H., Virden R., Hazlewood G.P., Henrissat B., Gilbert H.J.
Biochemistry 36:15489-15500(1997) [PubMed: 9398278] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], REACTION MECHANISM, INDUCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLU-161 AND GLU-270.
[2]"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: 18556790] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ueda107.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X91885 Genomic DNA. Translation: CAA62990.1.
CP000934 Genomic DNA. Translation: ACE83887.1.
RefSeqYP_001981020.1. NC_010995.1.

3D structure databases

ProteinModelPortalP48841.
ModBaseSearch...

Protein family/group databases

CAZyGH53. Glycoside Hydrolase Family 53.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6413839.
GenomeReviewsGene locus CJA_0497 in contig CP000934_GR.
KEGGcja:CJA_0497.
PATRIC21324375. VBICelJap122165_0507.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAIVSIGNE.
ProtClustDBCLSK570592.

Family and domain databases

InterProIPR011683. Glyco_hydro_53.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
KOK01224.
PfamPF07745. Glyco_hydro_53. 1 hit.
[Graphical view]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGANA_CELJU
AccessionPrimary (citable) accession number: P48841
Secondary accession number(s): B3PIY6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: January 25, 2012
This is version 56 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

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