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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        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
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: November 26, 2014
This is version 61 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