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Q09HN2

- BGAL_PLASL

UniProt

Q09HN2 - BGAL_PLASL

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Protein

Beta-galactosidase BgaP

Gene

bgaP

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

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.1 Publication

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei112 – 1121SubstrateBy similarity
Metal bindingi116 – 1161ZincBy similarity
Binding sitei150 – 1501SubstrateBy similarity
Active sitei151 – 1511Proton donorBy similarity
Metal bindingi156 – 1561ZincBy similarity
Metal bindingi158 – 1581ZincBy similarity
Metal bindingi161 – 1611ZincBy similarity
Active sitei308 – 3081NucleophileBy similarity
Binding sitei316 – 3161SubstrateBy 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-galBy similarity
Gene namesi
Name:bgaP1 Publication
Synonyms:galP1 Publication
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 BgaPPRO_0000407693Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ09HN2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Q09HN2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MINDKLPKIW HGGDYNPEQW DSQEIWDEDV RMFKLAGIDV ATLNVFSWAL
60 70 80 90 100
NQPNEDTYNF EWLDDKINRL YENGIYTCLA TSTAAHPAWM AKKYPDVLRV
110 120 130 140 150
DFYGRKRKFG SRHNSCPNSP TYREYSEKIA DKLAERYKDH PAVLIWHVSN
160 170 180 190 200
EYGGYCYCDN CQDAFRVWLS DKYGTLEKLN KAWNTGFWGH TFYEWDEIVA
210 220 230 240 250
PNMLSEERED NVSDFQGISL DYRRFQSDSL LDCYKLEYNA IRKHTPNIPI
260 270 280 290 300
TTNLMGTYPM LDYFKWAKEM DVVSWDNYPA IDTPFSYTAM THDLMRGLKS
310 320 330 340 350
GQPFMLMEQT PSQQNWQPYN SLKRPGVMRL WSYQAIGRGA DTILYFQLRR
360 370 380 390 400
SVGACEKYHG AVIEHVGHEH TRVFNEVAQI GKEFNQLGDT LLDARVNARV
410 420 430 440 450
AIVFDWENRW ATELSSGPSV SLDYVNEVHK YYDALYKLNV QVDMVGVEED
460 470 480 490 500
LSQYDVVIAP VLYMVKEGYA AKVESFVENG GTFITTFFSG IVNETDIVTL
510 520 530 540 550
GGYPGELRKV LGIWAEEIDA LHPDETNEIV VNGSRGSLSG SYSCNLLFDL
560 570 580 590 600
IHTEGAQAVA EYGSDFYQGM PVLTVNEFGK GKAWYVASSP DAEFLVDFLQ
610 620 630 640 650
TVCEEAGVEP LLSVPEGVET TERVKDGQTY LFVLNHNNKV ESIDLKDSQY
660 670
QELLSTQQLS GTVELEAKGV FILAKV
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: L4Imported.

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: October 1, 2014
This is version 30 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