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Q09HN2

- BGAL_PLASL

UniProt

Q09HN2 - BGAL_PLASL

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Protein
Beta-galactosidase BgaP
Gene
bgaP, galP
Organism
Planococcus sp. (strain L4)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Hydrolyzes lactose, o-nitrophenyl-beta-D-galactopyranoside (ONPG), p-nitrophenyl-beta-D-galactopyranoside (PNPG), 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-gal), o-nitrophenyl-beta-D-fucopyranoside, p-nitrophenyl-beta-D-mannoside, o-nitrophenyl-beta-D-glucoside, p-nitrophenyl-beta-D-xyloside, p-nitrophenyl-beta-D-cellobioside, p-nitrophenyl-beta-D-arabinoside, p-nitrophenyl-beta-D-lactoside, p-nitrophenyl-beta-D-galacturonide, p-nitrophenyl-beta-D-glucuronide and p-nitrophenyl-alpha-D-galactoside with highest level of activity with ONPG as substrate, intermediate level of activity with PNPG and lower levels of activity with all other chromogenic nitrophenyl analogs. Able to hydrolyze 34% of milk lactose after 60 minutes at 5 degrees Celsius.1 Publication

Catalytic activityi

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

Enzyme regulationi

No activity lost during treatment with 100 mM EDTA after 2 hours, and the addition of 1 mM MgCl2, 1 mM CaCl2 or 1 mM MnCl2 has no effect. However, the enzyme activity is inhibited by Zn2+, Cu2+, Ni2+ and Co2+ to different extents. Addition of Na+ or K+ slightly stimulates the enzyme activity at low concentrations and the optimal concentration is 250 mM. A further increase of their concentration of ions above the optimum value results in a decrease in enzyme activity. The enzyme is still active even in the presence of Na+ or K+ at a concentration up to 5 M.1 Publication

Kineticsi

  1. KM=5.4 mM for ONPG (at 5 degrees Celsius and at pH 6.8)1 Publication
  2. KM=3.8 mM for ONPG (at 10 degrees Celsius and at pH 6.8)
  3. KM=2.9 mM for ONPG (at 20 degrees Celsius and at pH 6.8)
  4. KM=20.4 mM for lactose (at 5 degrees Celsius and at pH 6.8)
  5. KM=11.2 mM for lactose (at 10 degrees Celsius and at pH 6.8)
  6. KM=10.4 mM for lactose (at 20 degrees Celsius and at pH 6.8)

pH dependencei

Optimum pH is 6.8. Exhibits above 80% of its maximal activity in the pH range 6.0-8.0 using ONPG as substrate at 20 degrees Celsius.

Temperature dependencei

Optimum temperature is 20 degrees Celsius. Lowering or raising the temperature from 20 degrees Celsius results in reduction of activity when ONPG is used as substrate. Rather stable at or below 25 degrees Celsius, but loses 58% of activity after 30 minutes at 40 degrees Celsius. Loses all activity in only 10 minutes at 45 degrees Celsius. Exhibits 27% of maximal activity even at 0 degrees Celsius, but enzyme activity decreases with a further increase in temperature until it is undetectable above 50 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei112 – 1121Substrate By similarity
Metal bindingi116 – 1161Zinc By similarity
Binding sitei150 – 1501Substrate By similarity
Active sitei151 – 1511Proton donor By similarity
Metal bindingi156 – 1561Zinc By similarity
Metal bindingi158 – 1581Zinc By similarity
Metal bindingi161 – 1611Zinc By similarity
Active sitei308 – 3081Nucleophile By similarity
Binding sitei316 – 3161Substrate By similarity

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 BgaP (EC:3.2.1.23)
Short name:
Beta-gal
Gene namesi
Name:bgaP
Synonyms:galP
OrganismiPlanococcus sp. (strain L4)
Taxonomic identifieri377621 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPlanococcaceaePlanococcus

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Biotechnological usei

Could conceivably be developed to fulfill the practical requirements to enable its use for lactose removal in milk and dairy products at low temperature or a reporter enzyme for psychrophilic genetic systems.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 676676Beta-galactosidase BgaP
PRO_0000407693Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ09HN2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni356 – 3594Substrate 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.

Q09HN2-1 [UniParc]FASTAAdd to Basket

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MINDKLPKIW HGGDYNPEQW DSQEIWDEDV RMFKLAGIDV ATLNVFSWAL    50
NQPNEDTYNF EWLDDKINRL YENGIYTCLA TSTAAHPAWM AKKYPDVLRV 100
DFYGRKRKFG SRHNSCPNSP TYREYSEKIA DKLAERYKDH PAVLIWHVSN 150
EYGGYCYCDN CQDAFRVWLS DKYGTLEKLN KAWNTGFWGH TFYEWDEIVA 200
PNMLSEERED NVSDFQGISL DYRRFQSDSL LDCYKLEYNA IRKHTPNIPI 250
TTNLMGTYPM LDYFKWAKEM DVVSWDNYPA IDTPFSYTAM THDLMRGLKS 300
GQPFMLMEQT PSQQNWQPYN SLKRPGVMRL WSYQAIGRGA DTILYFQLRR 350
SVGACEKYHG AVIEHVGHEH TRVFNEVAQI GKEFNQLGDT LLDARVNARV 400
AIVFDWENRW ATELSSGPSV SLDYVNEVHK YYDALYKLNV QVDMVGVEED 450
LSQYDVVIAP VLYMVKEGYA AKVESFVENG GTFITTFFSG IVNETDIVTL 500
GGYPGELRKV LGIWAEEIDA LHPDETNEIV VNGSRGSLSG SYSCNLLFDL 550
IHTEGAQAVA EYGSDFYQGM PVLTVNEFGK GKAWYVASSP DAEFLVDFLQ 600
TVCEEAGVEP LLSVPEGVET TERVKDGQTY LFVLNHNNKV ESIDLKDSQY 650
QELLSTQQLS GTVELEAKGV FILAKV 676
Length:676
Mass (Da):77,312
Last modified:October 17, 2006 - v1
Checksum:i6A2354F4544A752E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ899950 Genomic DNA. Translation: ABI64125.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ899950 Genomic DNA. Translation: ABI64125.1 .

3D structure databases

ProteinModelPortali Q09HN2.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH42. Glycoside Hydrolase Family 42.

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. "Molecular cloning and characterization of the gene encoding cold-active beta-galactosidase from a psychrotrophic and halotolerant Planococcus sp. L4."
    Hu J.M., Li H., Cao L.X., Wu P.C., Zhang C.T., Sang S.L., Zhang X.Y., Chen M.J., Lu J.Q., Liu Y.H.
    J. Agric. Food Chem. 55:2217-2224(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, BIOTECHNOLOGY.
    Strain: L4.

Entry informationi

Entry nameiBGAL_PLASL
AccessioniPrimary (citable) accession number: Q09HN2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: October 17, 2006
Last modified: June 11, 2014
This is version 29 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

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