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O69315

- BGAL_THETH

UniProt

O69315 - BGAL_THETH

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Protein
Beta-galactosidase
Gene
N/A
Organism
Thermus thermophilus
Status
Reviewed - 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)

pH dependencei

Optimum pH is 6.5. No activity is detected at pH below 4.5.

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.

Sites

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

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

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
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 645645Beta-galactosidase
PRO_0000367028Add
BLAST

Interactioni

Subunit structurei

Homotrimer.2 Publications

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiO69315.

Family & Domainsi

Region

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

Sequence similaritiesi

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...

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: June 11, 2014
This is version 59 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

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