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O31529

- BGAL1_BACSU

UniProt

O31529 - BGAL1_BACSU

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Protein
Beta-galactosidase YesZ
Gene
yesZ, BSU07080
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

May play a role in the degradation of rhamnogalacturonan derived from plant cell walls.1 Publication

Catalytic activityi

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

Kineticsi

  1. KM=3.0 mM for p-nitrophenyl beta-D-galactopyranoside (at pH 7.0 and 37 degrees Celsius)1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei106 – 1061Substrate By similarity
Metal bindingi110 – 1101Zinc By similarity
Binding sitei144 – 1441Substrate By similarity
Active sitei145 – 1451Proton donor Inferred
Metal bindingi153 – 1531Zinc By similarity
Metal bindingi155 – 1551Zinc By similarity
Metal bindingi158 – 1581Zinc By similarity
Active sitei296 – 2961Nucleophile Inferred

GO - Molecular functioni

  1. beta-galactosidase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. galactose metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU07080-MONOMER.
SABIO-RKO31529.

Protein family/group databases

CAZyiGH42. Glycoside Hydrolase Family 42.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-galactosidase YesZ (EC:3.2.1.23)
Short name:
Beta-gal
Alternative name(s):
Probable rhamnogalacturonan beta-galactosidase
Gene namesi
Name:yesZ
Ordered Locus Names:BSU07080
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU07080.

Subcellular locationi

GO - Cellular componenti

  1. beta-galactosidase complex Source: InterPro
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

No chromogen 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-Gal) hydrolyzation.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi145 – 1451E → A: Hydrolysis of the covalent glycosyl-enzyme intermediate is slowed. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 663663Beta-galactosidase YesZ
PRO_0000367024Add
BLAST

Proteomic databases

PaxDbiO31529.

Expressioni

Inductioni

Up-regulated by growth on type I rhamnogalacturonan.1 Publication

Interactioni

Subunit structurei

Homotrimer By similarity.

Protein-protein interaction databases

STRINGi224308.BSU07080.

Structurei

3D structure databases

ProteinModelPortaliO31529.
SMRiO31529. Positions 17-149.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni345 – 3484Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1874.
HOGENOMiHOG000095202.
KOiK01190.
OMAiMAKWAND.
OrthoDBiEOG6HMX9F.
PhylomeDBiO31529.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
3.40.50.880. 1 hit.
InterProiIPR013739. 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]
PfamiPF02449. Glyco_hydro_42. 1 hit.
PF08533. Glyco_hydro_42C. 1 hit.
PF08532. Glyco_hydro_42M. 1 hit.
[Graphical view]
PIRSFiPIRSF001084. B-galactosidase. 1 hit.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF52317. SSF52317. 1 hit.

Sequencei

Sequence statusi: Complete.

O31529-1 [UniParc]FASTAAdd to Basket

« Hide

MRKLYHGACY YPELWDEETI QQDIDIMREV GVNVVRIGEF AWSVMEPEEG    50
KIDVGFFKEI IARLYDSGIE TIMCTPTPTP PIWFSHGRPE RMHANEKREI 100
MGHGSRQHAC TNNPYFRKKA AIITTAIAKE LGRLPGLIGW QLDNEFKCHV 150
AECMCETCLR LWHDWLKNRY GVIERLNEAW GTDVWSETYQ TFEQVPQPGP 200
APFLHHASLR TMYQLFSMEM IASFADEQAK IIRCYSDAPI THNGSVMFSV 250
DNERMFQNLD FASYDTYASQ ENASAFLLNC DLWRNLKQGR PFWILETSPS 300
YAASLESSAY PHADGYLQAE AVSSYALGSQ GFCYWLWRQQ RSGSEISHGS 350
VLSAWGEPTI GYQNVLAVER ARKEIEPIIL STEPVQAEAA MTYSDRAKAF 400
IKTEPHRGLR HRSLVTHFYE RILNTGIHRD LIPEGAPLDG YRLLFTPFVP 450
YLSSEFIKKA SAFAEAGGIW ITGPLTGGRT CEHTIHTDCG LGELEKTSGI 500
KTLFTFPMNE NVNTGKAFGI TAPLGLWSAV FDTESGNTLG TVEAGPGAGH 550
AFLTERNYGE GKIVMLGSLP SGKEGDAMLE ALVRHYAEEA VISSRSDVTP 600
GTIVAPRIGE NGLVWIVVNM DGKGGSVTLP ESGTDLLTHR LEKAGRLAVG 650
PHEYRVIQFD NHS 663
Length:663
Mass (Da):74,099
Last modified:January 1, 1998 - v1
Checksum:i7E5799B02C0C5238
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL009126 Genomic DNA. Translation: CAB12527.1.
PIRiA69798.
RefSeqiNP_388589.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB12527; CAB12527; BSU07080.
GeneIDi936080.
KEGGibsu:BSU07080.
PATRICi18973064. VBIBacSub10457_0746.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL009126 Genomic DNA. Translation: CAB12527.1 .
PIRi A69798.
RefSeqi NP_388589.1. NC_000964.3.

3D structure databases

ProteinModelPortali O31529.
SMRi O31529. Positions 17-149.
ModBasei Search...

Protein-protein interaction databases

STRINGi 224308.BSU07080.

Protein family/group databases

CAZyi GH42. Glycoside Hydrolase Family 42.

Proteomic databases

PaxDbi O31529.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB12527 ; CAB12527 ; BSU07080 .
GeneIDi 936080.
KEGGi bsu:BSU07080.
PATRICi 18973064. VBIBacSub10457_0746.

Organism-specific databases

GenoListi BSU07080.

Phylogenomic databases

eggNOGi COG1874.
HOGENOMi HOG000095202.
KOi K01190.
OMAi MAKWAND.
OrthoDBi EOG6HMX9F.
PhylomeDBi O31529.

Enzyme and pathway databases

BioCyci BSUB:BSU07080-MONOMER.
SABIO-RK O31529.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
3.40.50.880. 1 hit.
InterProi IPR013739. 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 ]
Pfami PF02449. Glyco_hydro_42. 1 hit.
PF08533. Glyco_hydro_42C. 1 hit.
PF08532. Glyco_hydro_42M. 1 hit.
[Graphical view ]
PIRSFi PIRSF001084. B-galactosidase. 1 hit.
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF52317. SSF52317. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiBGAL1_BACSU
AccessioniPrimary (citable) accession number: O31529
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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