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O69315

- BGAL_THETH

UniProt

O69315 - BGAL_THETH

Protein

Beta-galactosidase

Gene
N/A
Organism
Thermus thermophilus
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Enzyme regulationi

    Inhibited by Cu2+ and Fe2+, and moderately activated by divalent cations such as Co2+, Mn2+ and Zn2+. Considerably activated by dithiothreitol, beta-mercaptoethanol and cysteine.1 Publication

    Kineticsi

    1. KM=19 mM for lactose (at pH 6.5 and at 70 degrees Celsius)1 Publication
    2. KM=5.9 mM for o-nitrophenyl beta-D-galactopyranoside (at pH 6.5 and at 70 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 6.5. No activity is detected at pH below 4.5.1 Publication

    Temperature dependencei

    Optimum temperature is 70 degrees Celsius. It retains more than 75% of activity after incubation at 85 degrees Celsius and the half-life at 90 degrees Celsius is 1 hour. Thermostable.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei102 – 1021Substrate1 Publication
    Metal bindingi106 – 1061Zinc
    Binding sitei140 – 1401Substrate1 Publication
    Active sitei141 – 1411Proton donor
    Metal bindingi150 – 1501Zinc
    Metal bindingi152 – 1521Zinc
    Metal bindingi155 – 1551Zinc
    Active sitei312 – 3121Nucleophile
    Binding sitei320 – 3201Substrate1 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

    Protein family/group databases

    CAZyiGH42. Glycoside Hydrolase Family 42.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-galactosidase (EC:3.2.1.23)
    Short name:
    Beta-gal
    Alternative name(s):
    Lactase
    OrganismiThermus thermophilus
    Taxonomic identifieri274 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

    Subcellular locationi

    GO - Cellular componenti

    1. beta-galactosidase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 645645Beta-galactosidasePRO_0000367028Add
    BLAST

    Interactioni

    Subunit structurei

    Homotrimer.2 Publications

    Structurei

    Secondary structure

    1
    645
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 54
    Helixi8 – 103
    Helixi13 – 153
    Helixi16 – 2611
    Beta strandi30 – 334
    Helixi38 – 414
    Helixi51 – 6111
    Turni62 – 643
    Beta strandi66 – 705
    Helixi78 – 836
    Helixi85 – 873
    Beta strandi99 – 1024
    Helixi110 – 12718
    Beta strandi133 – 1375
    Beta strandi139 – 1413
    Turni142 – 1465
    Helixi153 – 16715
    Helixi170 – 1778
    Turni178 – 1803
    Helixi181 – 1833
    Helixi189 – 1913
    Helixi204 – 23229
    Beta strandi237 – 2393
    Helixi251 – 2544
    Helixi255 – 2573
    Beta strandi258 – 2658
    Helixi267 – 2737
    Helixi278 – 2836
    Turni284 – 2874
    Helixi292 – 30312
    Turni304 – 3063
    Beta strandi308 – 3136
    Beta strandi319 – 3235
    Helixi331 – 34111
    Beta strandi347 – 3504
    Beta strandi356 – 3583
    Turni359 – 3624
    Helixi375 – 38814
    Beta strandi399 – 4035
    Helixi406 – 4149
    Helixi423 – 43513
    Turni436 – 4383
    Beta strandi441 – 4444
    Beta strandi454 – 4596
    Helixi466 – 4738
    Beta strandi479 – 4813
    Turni483 – 4864
    Helixi501 – 5055
    Beta strandi510 – 5167
    Beta strandi523 – 5275
    Beta strandi530 – 5345
    Beta strandi536 – 5427
    Beta strandi548 – 5514
    Beta strandi556 – 5616
    Beta strandi564 – 5674
    Helixi573 – 58614
    Beta strandi598 – 6036
    Beta strandi606 – 6116
    Beta strandi613 – 6153
    Beta strandi626 – 6305
    Beta strandi632 – 6343
    Beta strandi638 – 6436

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KWGX-ray1.60A1-645[»]
    1KWKX-ray2.20A1-645[»]
    ProteinModelPortaliO69315.
    SMRiO69315. Positions 1-644.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO69315.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni360 – 3634Substrate binding

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 42 family.Curated

    Family and domain databases

    Gene3Di2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    3.40.50.880. 1 hit.
    InterProiIPR013739. Beta_galactosidase_C.
    IPR013738. Beta_galactosidase_Trimer.
    IPR029062. Class_I_gatase-like.
    IPR013780. Glyco_hydro_13_b.
    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.

    O69315-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLGVCYYPEH WPKERWKEDA RRMREAGLSH VRIGEFAWAL LEPEPGRLEW    50
    GWLDEAIATL AAEGLKVVLG TPTATPPKWL VDRYPEILPV DREGRRRRFG 100
    GRRHYCFSSP VYREEARRIV TLLAERYGGL EAVAGFQTDN EYGCHDTVRC 150
    YCPRCQEAFR GWLEARYGTI EALNEAWGTA FWSQRYRSFA EVELPHLTVA 200
    EPNPSHLLDY YRFASDQVRA FNRLQVEILR AHAPGKFVTH NFMGFFTDLD 250
    AFALAQDLDF ASWDSYPLGF TDLMPLPPEE KLRYARTGHP DVAAFHHDLY 300
    RGVGRGRFWV MEQQPGPVNW APHNPSPAPG MVRLWTWEAL AHGAEVVSYF 350
    RWRQAPFAQE QMHAGLHRPD SAPDQGFFEA KRVAEELAAL ALPPVAQAPV 400
    ALVFDYEAAW IYEVQPQGAE WSYLGLVYLF YSALRRLGLD VDVVPPGASL 450
    RGYAFAVVPS LPIVREEALE AFREAEGPVL FGPRSGSKTE TFQIPKELPP 500
    GPLQALLPLK VVRVESLPPG LLEVAEGALG RFPLGLWREW VEAPLKPLLT 550
    FQDGKGALYR EGRYLYLAAW PSPELAGRLL SALAAEAGLK VLSLPEGLRL 600
    RRRGTWVFAF NYGPEAVEAP ASEGARFLLG SRRVGPYDLA VWEEA 645
    Length:645
    Mass (Da):72,824
    Last modified:August 1, 1998 - v1
    Checksum:i60FAE1EC1923C6C8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D85027 Genomic DNA. Translation: BAA28362.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D85027 Genomic DNA. Translation: BAA28362.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KWG X-ray 1.60 A 1-645 [» ]
    1KWK X-ray 2.20 A 1-645 [» ]
    ProteinModelPortali O69315.
    SMRi O69315. Positions 1-644.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH42. Glycoside Hydrolase Family 42.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei O69315.

    Family and domain databases

    Gene3Di 2.60.40.1180. 1 hit.
    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.
    IPR013780. Glyco_hydro_13_b.
    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. "Thermostable beta-galactosidase from an extreme thermophile, Thermus sp. A4: enzyme purification and characterization, and gene cloning and sequencing."
      Ohtsu N., Motoshima H., Goto K., Tsukasaki F., Matsuzawa H.
      Biosci. Biotechnol. Biochem. 62:1539-1545(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-15, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
      Strain: A4.
    2. "Trimeric crystal structure of the glycoside hydrolase family 42 beta-galactosidase from Thermus thermophilus A4 and the structure of its complex with galactose."
      Hidaka M., Fushinobu S., Ohtsu N., Motoshima H., Matsuzawa H., Shoun H., Wakagi T.
      J. Mol. Biol. 322:79-91(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH ZINC ION AND SUBSTRATE, REACTION MECHANISM, SUBUNIT.

    Entry informationi

    Entry nameiBGAL_THETH
    AccessioniPrimary (citable) accession number: O69315
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 60 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The trimeric structure is essential to exhibit high enzymatic activity.

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3