Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot O07013 (GANA_BACSU)

Last modified June 16, 2009. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: galA
Synonyms: yvfO
Ordered Locus Names: BSU34120
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length429 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. Ref.4

Catalytic activity

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

Cofactor

Binds 1 calcium ion per subunit By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 53 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 429408Arabinogalactan endo-1,4-beta-galactosidase
PRO_0000012222

Regions

Region146 – 1494Substrate binding By similarity
Region233 – 2342Substrate binding By similarity

Sites

Active site1941Proton donor By similarity
Active site2921Nucleophile By similarity
Metal binding3031Calcium By similarity
Metal binding3051Calcium By similarity
Metal binding3071Calcium By similarity
Metal binding3961Calcium By similarity
Metal binding3991Calcium By similarity
Binding site2671Substrate By similarity
Binding site2961Substrate By similarity
Binding site3111Substrate By similarity
Binding site3881Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
O07013-1 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 8A32869EA42127AD

FASTA42947,279
        10         20         30         40         50         60 
MKSKVKMFFA AAIVWSACSS TGYAAAIEKE KHVSELRAED LFVKKVEGMN KDFIKGADVS 

        70         80         90        100        110        120 
SVIALENSGV TFYNTNGKRQ DIFTTLKQAG VNYVRVRIWN HPYDSNGNGY GGGNNDVQKA 

       130        140        150        160        170        180 
IEIGKRATAN GMKVLADFHY SDFWADPAKQ KVPKAWANLS FEAKKAKLYE YTKQSLQKMI 

       190        200        210        220        230        240 
KEGVDIGMVQ VGNETTGGFA GETDWTKMCQ LFNEGSRAVR ETNSNILVAL HFTNPETAGR 

       250        260        270        280        290        300 
YSFIAETLSK NKVDYDVFAS SYYPFWHGTL QNLTSVLKAV ANTYGKKVMV AETSYTYTAE 

       310        320        330        340        350        360 
DGDGHGNTAP KSGQTLPYPI SVQGQATAVR DVMEAVANTG KAGLGVFYWE PAWIPVGPKT 

       370        380        390        400        410        420 
QIEKNKVLWE TYGSGWASSY AAEYDPEDAG KWYGGSAVDN QALFDFNGHP LPSLQVFQYA 


ESGHIPKKR 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of the lacA gene encoding beta-galactosidase in Bacillus subtilis and a regulator gene, lacR."
Daniel R.A., Haiech J., Denizot F., Errington J.
J. Bacteriol. 179:5636-5638(1997) [PubMed: 9287030] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]Denizot F.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[4]"Bioinformatic, genetic, and biochemical evidence that some glycoside hydrolase family 42 beta-galactosidases are arabinogalactan type I oligomer hydrolases."
Shipkowski S., Brenchley J.E.
Appl. Environ. Microbiol. 72:7730-7738(2006) [PubMed: 17056685] [Abstract]
Cited for: FUNCTION IN GALACTAN DEGRADATION.

Cross-references

Sequence databases

Z94043 Genomic DNA. Translation: CAB08009.1.
AL009126 Genomic DNA. Translation: CAB15417.2.
PIRF70038.
RefSeqNP_391292.2.

3D structure databases

HSSPHSSP built from PDB template 1FOB based on UniProtKB P48842.
SMRO07013. Positions 41-423.
ModBaseSearch...

Protein family/group databases

CAZyGH53. Glycoside Hydrolase Family 53.

Genome annotation databases

GeneID937086.
GenomeReviewsGene locus BSU34120 in contig AL009126_GR.
KEGGbsu:BSU34120.
NMPDRfig|224308.1.peg.3418.

Organism-specific databases

SubtiListBG12440. galA. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMO07013.
OMAO07013. EGKSWGQ.

Enzyme and pathway databases

BioCycBSUB224308:BSU3409-MON.

Family and domain databases

InterProIPR011683. Glyco_hydro_53.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF07745. Glyco_hydro_53. 1 hit.
[Graphical view]
PROSITEPS51257. PROKAR_LIPOPROTEIN. 1 hit. Uncertain.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGANA_BACSU
AccessionPrimary (citable) accession number: O07013
Secondary accession number(s): O32260
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 1, 1997
Last modified: June 16, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents