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Protein

Beta-galactosidase

Gene
N/A
Organism
Thermus thermophilus
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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)DescriptionActionsGraphical viewLength
    Binding sitei102Substrate1 Publication1
    Metal bindingi106Zinc1
    Binding sitei140Substrate1 Publication1
    Active sitei141Proton donor1
    Metal bindingi150Zinc1
    Metal bindingi152Zinc1
    Metal bindingi155Zinc1
    Active sitei312Nucleophile1
    Binding sitei320Substrate1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    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

    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00003670281 – 645Beta-galactosidaseAdd BLAST645

    Interactioni

    Subunit structurei

    Homotrimer.2 Publications

    Structurei

    Secondary structure

    1645
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 5Combined sources4
    Helixi8 – 10Combined sources3
    Helixi13 – 15Combined sources3
    Helixi16 – 26Combined sources11
    Beta strandi30 – 33Combined sources4
    Helixi38 – 41Combined sources4
    Helixi51 – 61Combined sources11
    Turni62 – 64Combined sources3
    Beta strandi66 – 70Combined sources5
    Helixi78 – 83Combined sources6
    Helixi85 – 87Combined sources3
    Beta strandi99 – 102Combined sources4
    Helixi110 – 127Combined sources18
    Beta strandi133 – 137Combined sources5
    Beta strandi139 – 141Combined sources3
    Turni142 – 146Combined sources5
    Helixi153 – 167Combined sources15
    Helixi170 – 177Combined sources8
    Turni178 – 180Combined sources3
    Helixi181 – 183Combined sources3
    Helixi189 – 191Combined sources3
    Helixi204 – 232Combined sources29
    Beta strandi237 – 239Combined sources3
    Helixi251 – 254Combined sources4
    Helixi255 – 257Combined sources3
    Beta strandi258 – 265Combined sources8
    Helixi267 – 273Combined sources7
    Helixi278 – 283Combined sources6
    Turni284 – 287Combined sources4
    Helixi292 – 303Combined sources12
    Turni304 – 306Combined sources3
    Beta strandi308 – 313Combined sources6
    Beta strandi319 – 323Combined sources5
    Helixi331 – 341Combined sources11
    Beta strandi347 – 350Combined sources4
    Beta strandi356 – 358Combined sources3
    Turni359 – 362Combined sources4
    Helixi375 – 388Combined sources14
    Beta strandi399 – 403Combined sources5
    Helixi406 – 414Combined sources9
    Helixi423 – 435Combined sources13
    Turni436 – 438Combined sources3
    Beta strandi441 – 444Combined sources4
    Beta strandi454 – 459Combined sources6
    Helixi466 – 473Combined sources8
    Beta strandi479 – 481Combined sources3
    Turni483 – 486Combined sources4
    Helixi501 – 505Combined sources5
    Beta strandi510 – 516Combined sources7
    Beta strandi523 – 527Combined sources5
    Beta strandi530 – 534Combined sources5
    Beta strandi536 – 542Combined sources7
    Beta strandi548 – 551Combined sources4
    Beta strandi556 – 561Combined sources6
    Beta strandi564 – 567Combined sources4
    Helixi573 – 586Combined sources14
    Beta strandi598 – 603Combined sources6
    Beta strandi606 – 611Combined sources6
    Beta strandi613 – 615Combined sources3
    Beta strandi626 – 630Combined sources5
    Beta strandi632 – 634Combined sources3
    Beta strandi638 – 643Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1KWGX-ray1.60A1-645[»]
    1KWKX-ray2.20A1-645[»]
    ProteinModelPortaliO69315.
    SMRiO69315.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO69315.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni360 – 363Substrate binding4

    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.
    IPR003476. Glyco_hydro_42.
    IPR013529. Glyco_hydro_42_N.
    IPR013780. Glyco_hydro_b.
    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

            10         20         30         40         50
    MLGVCYYPEH WPKERWKEDA RRMREAGLSH VRIGEFAWAL LEPEPGRLEW
    60 70 80 90 100
    GWLDEAIATL AAEGLKVVLG TPTATPPKWL VDRYPEILPV DREGRRRRFG
    110 120 130 140 150
    GRRHYCFSSP VYREEARRIV TLLAERYGGL EAVAGFQTDN EYGCHDTVRC
    160 170 180 190 200
    YCPRCQEAFR GWLEARYGTI EALNEAWGTA FWSQRYRSFA EVELPHLTVA
    210 220 230 240 250
    EPNPSHLLDY YRFASDQVRA FNRLQVEILR AHAPGKFVTH NFMGFFTDLD
    260 270 280 290 300
    AFALAQDLDF ASWDSYPLGF TDLMPLPPEE KLRYARTGHP DVAAFHHDLY
    310 320 330 340 350
    RGVGRGRFWV MEQQPGPVNW APHNPSPAPG MVRLWTWEAL AHGAEVVSYF
    360 370 380 390 400
    RWRQAPFAQE QMHAGLHRPD SAPDQGFFEA KRVAEELAAL ALPPVAQAPV
    410 420 430 440 450
    ALVFDYEAAW IYEVQPQGAE WSYLGLVYLF YSALRRLGLD VDVVPPGASL
    460 470 480 490 500
    RGYAFAVVPS LPIVREEALE AFREAEGPVL FGPRSGSKTE TFQIPKELPP
    510 520 530 540 550
    GPLQALLPLK VVRVESLPPG LLEVAEGALG RFPLGLWREW VEAPLKPLLT
    560 570 580 590 600
    FQDGKGALYR EGRYLYLAAW PSPELAGRLL SALAAEAGLK VLSLPEGLRL
    610 620 630 640
    RRRGTWVFAF NYGPEAVEAP ASEGARFLLG SRRVGPYDLA VWEEA
    Length:645
    Mass (Da):72,824
    Last modified:August 1, 1998 - v1
    Checksum:i60FAE1EC1923C6C8
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D85027 Genomic DNA. Translation: BAA28362.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D85027 Genomic DNA. Translation: BAA28362.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1KWGX-ray1.60A1-645[»]
    1KWKX-ray2.20A1-645[»]
    ProteinModelPortaliO69315.
    SMRiO69315.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiGH42. Glycoside Hydrolase Family 42.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Miscellaneous databases

    EvolutionaryTraceiO69315.

    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.
    IPR003476. Glyco_hydro_42.
    IPR013529. Glyco_hydro_42_N.
    IPR013780. Glyco_hydro_b.
    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.
    ProtoNetiSearch...

    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: November 2, 2016
    This is version 68 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.