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O31529

- BGAL1_BACSU

UniProt

O31529 - BGAL1_BACSU

Protein

Beta-galactosidase YesZ

Gene

yesZ

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    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 – 1061SubstrateBy similarity
    Metal bindingi110 – 1101ZincBy similarity
    Binding sitei144 – 1441SubstrateBy similarity
    Active sitei145 – 1451Proton donor1 Publication
    Metal bindingi153 – 1531ZincBy similarity
    Metal bindingi155 – 1551ZincBy similarity
    Metal bindingi158 – 1581ZincBy similarity
    Active sitei296 – 2961Nucleophile1 Publication

    GO - Molecular functioni

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

    GO - Biological processi

    1. galactose metabolic process Source: InterPro

    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

    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 YesZPRO_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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 42 family.Curated

    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 79 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