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O31529 (BGAL1_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 78. 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:
Beta-galactosidase YesZ

Short name=Beta-gal
EC=3.2.1.23
Alternative name(s):
Probable rhamnogalacturonan beta-galactosidase
Gene names
Name:yesZ
Ordered Locus Names:BSU07080
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length663 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in the degradation of rhamnogalacturonan derived from plant cell walls. Ref.3

Catalytic activity

Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.

Subunit structure

Homotrimer By similarity.

Induction

Up-regulated by growth on type I rhamnogalacturonan. Ref.3

Disruption phenotype

No chromogen 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-Gal) hydrolyzation. Ref.2

Sequence similarities

Belongs to the glycosyl hydrolase 42 family.

Biophysicochemical properties

Kinetic parameters:

KM=3.0 mM for p-nitrophenyl beta-D-galactopyranoside (at pH 7.0 and 37 degrees Celsius) Ref.4

Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processgalactose metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentbeta-galactosidase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionbeta-galactosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 663663Beta-galactosidase YesZ
PRO_0000367024

Regions

Region345 – 3484Substrate binding By similarity

Sites

Active site1451Proton donor Probable
Active site2961Nucleophile Probable
Metal binding1101Zinc By similarity
Metal binding1531Zinc By similarity
Metal binding1551Zinc By similarity
Metal binding1581Zinc By similarity
Binding site1061Substrate By similarity
Binding site1441Substrate By similarity

Experimental info

Mutagenesis1451E → A: Hydrolysis of the covalent glycosyl-enzyme intermediate is slowed. Ref.4

Sequences

Sequence LengthMass (Da)Tools
O31529 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 7E5799B02C0C5238

FASTA66374,099
        10         20         30         40         50         60 
MRKLYHGACY YPELWDEETI QQDIDIMREV GVNVVRIGEF AWSVMEPEEG KIDVGFFKEI 

        70         80         90        100        110        120 
IARLYDSGIE TIMCTPTPTP PIWFSHGRPE RMHANEKREI MGHGSRQHAC TNNPYFRKKA 

       130        140        150        160        170        180 
AIITTAIAKE LGRLPGLIGW QLDNEFKCHV AECMCETCLR LWHDWLKNRY GVIERLNEAW 

       190        200        210        220        230        240 
GTDVWSETYQ TFEQVPQPGP APFLHHASLR TMYQLFSMEM IASFADEQAK IIRCYSDAPI 

       250        260        270        280        290        300 
THNGSVMFSV DNERMFQNLD FASYDTYASQ ENASAFLLNC DLWRNLKQGR PFWILETSPS 

       310        320        330        340        350        360 
YAASLESSAY PHADGYLQAE AVSSYALGSQ GFCYWLWRQQ RSGSEISHGS VLSAWGEPTI 

       370        380        390        400        410        420 
GYQNVLAVER ARKEIEPIIL STEPVQAEAA MTYSDRAKAF IKTEPHRGLR HRSLVTHFYE 

       430        440        450        460        470        480 
RILNTGIHRD LIPEGAPLDG YRLLFTPFVP YLSSEFIKKA SAFAEAGGIW ITGPLTGGRT 

       490        500        510        520        530        540 
CEHTIHTDCG LGELEKTSGI KTLFTFPMNE NVNTGKAFGI TAPLGLWSAV FDTESGNTLG 

       550        560        570        580        590        600 
TVEAGPGAGH AFLTERNYGE GKIVMLGSLP SGKEGDAMLE ALVRHYAEEA VISSRSDVTP 

       610        620        630        640        650        660 
GTIVAPRIGE NGLVWIVVNM DGKGGSVTLP ESGTDLLTHR LEKAGRLAVG PHEYRVIQFD 


NHS 

« Hide

References

« Hide 'large scale' references
[1]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[2]"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] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[3]"Plant cell wall degradation by saprophytic Bacillus subtilis strains: gene clusters responsible for rhamnogalacturonan depolymerization."
Ochiai A., Itoh T., Kawamata A., Hashimoto W., Murata K.
Appl. Environ. Microbiol. 73:3803-3813(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DEGRADATION OF TYPE I RHAMNOGALACTURONAN, INDUCTION.
Strain: 168.
[4]"Identification of the catalytic nucleophile in family 42 beta-galactosidases by intermediate trapping and peptide mapping: YesZ from Bacillus subtilis."
Shaikh F.A., Muellegger J., He S., Withers S.G.
FEBS Lett. 581:2441-2446(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, MUTAGENESIS OF GLU-145.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL009126 Genomic DNA. Translation: CAB12527.1.
PIRA69798.
RefSeqNP_388589.1. NC_000964.3.

3D structure databases

ProteinModelPortalO31529.
SMRO31529. Positions 17-149.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU07080.

Protein family/group databases

CAZyGH42. Glycoside Hydrolase Family 42.

Proteomic databases

PaxDbO31529.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB12527; CAB12527; BSU07080.
GeneID936080.
KEGGbsu:BSU07080.
PATRIC18973064. VBIBacSub10457_0746.

Organism-specific databases

GenoListBSU07080.

Phylogenomic databases

eggNOGCOG1874.
HOGENOMHOG000095202.
KOK01190.
OMAMAKWAND.
OrthoDBEOG6HMX9F.
PhylomeDBO31529.

Enzyme and pathway databases

BioCycBSUB:BSU07080-MONOMER.
SABIO-RKO31529.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
3.40.50.880. 1 hit.
InterProIPR013739. Beta_galactosidase_C.
IPR013738. Beta_galactosidase_Trimer.
IPR029062. Class_I_gatase-like.
IPR003476. Glyco_hydro_42.
IPR013529. Glyco_hydro_42_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF02449. Glyco_hydro_42. 1 hit.
PF08533. Glyco_hydro_42C. 1 hit.
PF08532. Glyco_hydro_42M. 1 hit.
[Graphical view]
PIRSFPIRSF001084. B-galactosidase. 1 hit.
SUPFAMSSF51445. SSF51445. 1 hit.
SSF52317. SSF52317. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBGAL1_BACSU
AccessionPrimary (citable) accession number: O31529
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 78 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Bacillus subtilis

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