SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

C7ASJ5

- BGAL2_ARTSP

UniProt

C7ASJ5 - BGAL2_ARTSP

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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.

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei144 – 1441Substrate By similarity
Binding sitei182 – 1821Substrate By similarity
Active sitei183 – 1831Proton donor By similarity
Active sitei341 – 3411Nucleophile By similarity
Binding sitei349 – 3491Substrate By similarity

GO - Molecular functioni

  1. beta-galactosidase activity Source: UniProtKB-EC
Complete GO annotation...

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-gal
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-galactosidase
PRO_0000407681Add
BLAST

Interactioni

Subunit structurei

Homotrimer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliC7ASJ5.

Family & Domainsi

Region

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

Sequence similaritiesi

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

MGKRFPSGWF SPRVHPPRRQ RSPMTNQATP GTASVWNNIE GIGFGGDYNP    50
EQWPVSVRLE DLELMQEAGV NFLSVGIFSW ALLEPAEGQY DFGWLDDVMD 100
NLHGIGVKVA LATATAAPPA WLVRKHPEIL PVTADGTTLG PGSRRHYTPS 150
SAVYRKYAAG ITRVLAERYK DHPALALWHV DNELGCHVSE FYGEEDAAAF 200
RLWLERRYGT IDALNAAWGT AFWSQHYGSF EEILPPGVAP STLNPGQQLD 250
FQRFNSWALM DYYRSLVAVL REVTPAVPCT TNLMASSATK SMDYFSWAKD 300
LDVIANDHYL VAADPERHIE LAFSADLTRG IAGGDPWILM EHSTSAVNWQ 350
PRNQPKMPGE MLRNSLAHVA RGADAVMFFQ WRQSFAGSEK FHSAMVPHGG 400
RDTRVWREVV DLGAALQLLA PVRGSRVESR AAIVFDYEAW WASEIDSKPS 450
IDVRYLDLLR AFHRSLFLRG VSVDMVHPSA SLDGYDLVLV CTLYSVTDEA 500
AANIAAAAAG GATVLVSYFS GITDEKDHVR LGGYPGAFRE LLGVRVEEFH 550
PLLAGSQLKL SDGTVSSIWS EHVHLDGAEA FQTFTGYPLE GVPSLTRRAV 600
GTGAAWYLAT FPDRDGIESL VDRLLAESGV SPVAEADAGV ELTRRRSADG 650
GSFLFAINHT RAAASVRASG TDVLSGERFT GTVEAGSVAV IAED 694
Length:694
Mass (Da):75,915
Last modified:September 22, 2009 - v1
Checksum:i2A352EDCF797BE74
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FJ609657 Genomic DNA. Translation: ACU00913.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FJ609657 Genomic DNA. Translation: ACU00913.1 .

3D structure databases

ProteinModelPortali C7ASJ5.
ModBasei 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: 32c.

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: June 11, 2014
This is version 14 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

Similar proteinsi