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Q65CX5 (GANA_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 63. Feed History...

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

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:galA, yvfO
Ordered Locus Names:BLi04276, BL00263
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes the beta-1,4-galactan linkages of arabinogalactan type I, a pectic substance found in plants such as soybeans.

Catalytic activity

The enzyme specifically hydrolyzes (1->4)-beta-D-galactosidic linkages in type I arabinogalactans.

Cofactor

Binds 1 calcium ion per subunit. Ref.3

Sequence similarities

Belongs to the glycosyl hydrolase 53 family.

Sequence caution

The sequence AAU25711.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 424398Arabinogalactan endo-1,4-beta-galactosidase
PRO_0000371562

Regions

Region142 – 1454Substrate binding
Region229 – 2302Substrate binding

Sites

Active site1901Proton donor Probable
Active site2881Nucleophile Probable
Metal binding2991Calcium
Metal binding3011Calcium
Metal binding3031Calcium
Metal binding3921Calcium
Metal binding3951Calcium
Binding site2631Substrate
Binding site2921Substrate
Binding site3071Substrate
Binding site3841Substrate

Secondary structure

................................................................ 424
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q65CX5 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: E6CC3D0D1B80D166

FASTA42446,225
        10         20         30         40         50         60 
MKNVLAVFVV LIFVLGAFGT SGPAEAARDS GTAKSGLYVE KVSGLRKDFI KGVDVSSIIA 

        70         80         90        100        110        120 
LEESGVAFYN ESGKKQDIFK TLKEAGVNYV RVRIWNDPYD ANGNGYGGGN NDLEKAIQIG 

       130        140        150        160        170        180 
KRATANGMKL LADFHYSDFW ADPAKQKAPK AWANLNFEDK KTALYQYTKQ SLKAMKAAGI 

       190        200        210        220        230        240 
DIGMVQVGNE TNGGLAGETD WAKMSQLFNA GSQAVRETDS NILVALHFTN PETSGRYAWI 

       250        260        270        280        290        300 
AETLHRHHVD YDVFASSYYP FWHGTLKNLT SVLTSVADTY GKKVMVAETS YTYTAEDGDG 

       310        320        330        340        350        360 
HGNTAPKNGQ TLNNPVTVQG QANAVRDVIQ AVSDVGEAGI GVFYWEPAWI PVGPAHRLEK 

       370        380        390        400        410        420 
NKALWETYGS GWATSYAAEY DPEDAGKWFG GSAVDNQALF DFKGRPLPSL HVFQYVDTGT 


PFKN 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[3]"The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products."
Ryttersgaard C., Le Nours J., Lo Leggio L., Joergensen C.T., Christensen L.L., Bjoernvad M., Larsen S.
J. Mol. Biol. 341:107-117(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 28-424 IN COMPLEX WITH CALCIUM IONS AND SUBSTRATE ANALOGS, COFACTOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017333 Genomic DNA. Translation: AAU43089.1.
CP000002 Genomic DNA. Translation: AAU25711.1. Different initiation.
RefSeqYP_006715543.1. NC_006322.1.
YP_081349.1. NC_006270.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1R8LX-ray2.60A/B28-424[»]
1UR0X-ray2.50A/B28-424[»]
1UR4X-ray2.20A/B28-424[»]
2CCRX-ray2.30A/B28-424[»]
2GFTX-ray2.30A/B28-424[»]
2J74X-ray2.60A/B28-424[»]
ProteinModelPortalQ65CX5.
SMRQ65CX5. Positions 36-422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279010.BL00263.

Protein family/group databases

CAZyGH53. Glycoside Hydrolase Family 53.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU25711; AAU25711; BL00263.
AAU43089; AAU43089; BLi04276.
GeneID3029947.
3101427.
KEGGbld:BLi04276.
bli:BL00263.
PATRIC18954382. VBIBacLic203714_4366.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3867.
HOGENOMHOG000118034.
KOK01224.
OMARWWFDEI.
OrthoDBEOG6H4K5M.
ProtClustDBCLSK764973.

Enzyme and pathway databases

BioCycBLIC279010:GJ2P-4230-MONOMER.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR011683. Glyco_hydro_53.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF07745. Glyco_hydro_53. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ65CX5.

Entry information

Entry nameGANA_BACLD
AccessionPrimary (citable) accession number: Q65CX5
Secondary accession number(s): Q62NF0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: October 25, 2004
Last modified: November 13, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries