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C7ASJ5

- BGAL2_ARTSP

UniProt

C7ASJ5 - BGAL2_ARTSP

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Protein

Beta-galactosidase

Gene
N/A
Organism
Arthrobacter sp.
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Hydrolyzes p-nitrophenyl-beta-D-galactopyranoside (PNPG), o-nitrophenyl-beta-D-galactopyranoside (ONPG) and chromogen 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-gal), with highest activity against PNPG. Also acts on p-nitrophenyl-beta-D-glucopyranoside (PNPGlu) and o-nitrophenyl-beta-D-glucopyranoside (ONPGlu), but with significantly lower activity.1 Publication

Catalytic activityi

Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.1 Publication

Enzyme regulationi

Strongly inhibited by glucose. No activity is lost during treatment with 100 mM EDTA after 2 hours. Activity not considerably affected by metal ions (5 mM), including Na+, K+, Mg2+, Co2+ and Ca2+. Completely inhibited by Cu2+ and Zn2+ (5 mM) and is strongly inhibited by Mn2+ (11%), Fe2+ (25%) and Ni2+ (38%) in comparison with the activity in the absence of cations (100%). Activity not affected by dithiothreitol, beta-mercaptoethanol and L-cysteine whereas reduced glutathione almost completely inactivates it. With ONPG as substrate, the addition of ethanol up to 20% still slightly stimulates activity. The activity increases up to 120% in the presence of 8% v/v ethanol at pH 5.5.1 Publication

Kineticsi

  1. KM=5.75 mM for ONPG (at 10 degrees Celsius)1 Publication
  2. KM=4.86 mM for ONPG (at 20 degrees Celsius)1 Publication
  3. KM=3.46 mM for ONPG (at 30 degrees Celsius)1 Publication
  4. KM=3.15 mM for ONPG (at 40 degrees Celsius)1 Publication
  5. KM=2.62 mM for ONPG (at 50 degrees Celsius)1 Publication
  6. KM=5.11 mM for ONPG (at 55 degrees Celsius)1 Publication
  7. KM=77.54 mM for lactose (at 10 degrees Celsius)1 Publication
  8. KM=67.82 mM for lactose (at 20 degrees Celsius)1 Publication
  9. KM=52.67 mM for lactose (at 30 degrees Celsius)1 Publication
  10. KM=44.31 mM for lactose (at 40 degrees Celsius)1 Publication
  11. KM=39.73 mM for lactose (at 50 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 6.5 with ONPG as substrate. Over 90% of activity in the pH range 6.5-8.5. Highly efficient at pH range 4.5-9.5.1 Publication

Temperature dependencei

Optimum temperature is 50 degrees Celsius with ONPG as substrate. Active at 4-8 degrees Celsius. 60% of the maximum activity is detected at 25 degrees Celsius and 15% at 0 degrees Celsius. Over 50% activity at 30 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei144 – 1441SubstrateBy similarity
Binding sitei182 – 1821SubstrateBy similarity
Active sitei183 – 1831Proton donorBy similarity
Active sitei341 – 3411NucleophileBy similarity
Binding sitei349 – 3491SubstrateBy similarity

GO - Molecular functioni

  1. beta-galactosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. galactose metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-galactosidase (EC:3.2.1.23)
Short name:
Beta-galBy similarity
OrganismiArthrobacter sp.
Taxonomic identifieri1667 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

Subcellular locationi

GO - Cellular componenti

  1. beta-galactosidase complex Source: InterPro
Complete GO annotation...

Pathology & Biotechi

Biotechnological usei

Has potential use in lactose removal in milk and dairy products at low temperatures and for cheese whey bioremediation processes with simultaneous bio-ethanol production.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 694694Beta-galactosidasePRO_0000407681Add
BLAST

Interactioni

Subunit structurei

Homotrimer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliC7ASJ5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni389 – 3924Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 42 family.Sequence Analysis

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.

C7ASJ5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGKRFPSGWF SPRVHPPRRQ RSPMTNQATP GTASVWNNIE GIGFGGDYNP
60 70 80 90 100
EQWPVSVRLE DLELMQEAGV NFLSVGIFSW ALLEPAEGQY DFGWLDDVMD
110 120 130 140 150
NLHGIGVKVA LATATAAPPA WLVRKHPEIL PVTADGTTLG PGSRRHYTPS
160 170 180 190 200
SAVYRKYAAG ITRVLAERYK DHPALALWHV DNELGCHVSE FYGEEDAAAF
210 220 230 240 250
RLWLERRYGT IDALNAAWGT AFWSQHYGSF EEILPPGVAP STLNPGQQLD
260 270 280 290 300
FQRFNSWALM DYYRSLVAVL REVTPAVPCT TNLMASSATK SMDYFSWAKD
310 320 330 340 350
LDVIANDHYL VAADPERHIE LAFSADLTRG IAGGDPWILM EHSTSAVNWQ
360 370 380 390 400
PRNQPKMPGE MLRNSLAHVA RGADAVMFFQ WRQSFAGSEK FHSAMVPHGG
410 420 430 440 450
RDTRVWREVV DLGAALQLLA PVRGSRVESR AAIVFDYEAW WASEIDSKPS
460 470 480 490 500
IDVRYLDLLR AFHRSLFLRG VSVDMVHPSA SLDGYDLVLV CTLYSVTDEA
510 520 530 540 550
AANIAAAAAG GATVLVSYFS GITDEKDHVR LGGYPGAFRE LLGVRVEEFH
560 570 580 590 600
PLLAGSQLKL SDGTVSSIWS EHVHLDGAEA FQTFTGYPLE GVPSLTRRAV
610 620 630 640 650
GTGAAWYLAT FPDRDGIESL VDRLLAESGV SPVAEADAGV ELTRRRSADG
660 670 680 690
GSFLFAINHT RAAASVRASG TDVLSGERFT GTVEAGSVAV IAED
Length:694
Mass (Da):75,915
Last modified:September 22, 2009 - v1
Checksum:i2A352EDCF797BE74
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ609657 Genomic DNA. Translation: ACU00913.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ609657 Genomic DNA. Translation: ACU00913.1 .

3D structure databases

ProteinModelPortali C7ASJ5.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

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. "A new cold-adapted beta-D-galactosidase from the Antarctic Arthrobacter sp. 32c - gene cloning, overexpression, purification and properties."
    Hildebrandt P., Wanarska M., Kur J.
    BMC Microbiol. 9:151-151(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, BIOTECHNOLOGY.
    Strain: 32cImported.

Entry informationi

Entry nameiBGAL2_ARTSP
AccessioniPrimary (citable) accession number: C7ASJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: September 22, 2009
Last modified: October 1, 2014
This is version 15 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3