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Q9KI47

- BGAL_PLASS

UniProt

Q9KI47 - BGAL_PLASS

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Protein

Beta-galactosidase BgaA

Gene
bgaA
Organism
Planococcus sp. (strain 'SOS Orange')
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Hydrolyzes o-nitrophenyl-beta-D-galactopyranoside (ONPG), p-nitrophenyl-beta-D-galactopyranoside (PNPG), 5-bromo-4-chloro-3-indoyl-beta-D-galactosde (X-gal), o-nitrophenyl-beta-D-fucopyranoside (ONPF) and p-nitrophenyl-beta-D-fucopyranoside (PNPF) with greatest activity towards ONPG and PNPG and low levels of activity with ONPF and PNPF. Detectable, but very low levels of activity towards p-nitrophenyl-beta-lactose (PNPL), p-nitrophenyl-beta-cellobiose (PNPC), p-nitrophenyl-alpha-galactopyranoside (PNP-alpha-G), and p-nitrophenyl-beta-xylopyranoside (PNPX).1 Publication

Catalytic activityi

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

Enzyme regulationi

No activity is lost during treatment with 20 or 100 mM EDTA in Z buffer for 3 hours at 0 degrees Celsius, nor is activity greatly stimulated by the addition of cations. Inhibited by 1 mM zinc and 1 mM copper, the levels of activity decrease to 10% of the untreated control. Nickel, cobalt and manganese at concentrations of 10 mM decrease enzyme activity to either 40% (for nickel and cobalt) or 60% (for manganese) of the activity in untreated controls. No change in enzyme activity in the presence of calcium and magnesium at concentrations up to 50 mM. EDTA-treated enzyme exhibits a slight increase in relative specific activity when it is assayed in the presence of 50 mM NaCl or 50 mM KCl, it does not exhibit enhanced activity at concentrations greater than 250 mM. Maintains between 20 and 40% of activity in the presence of 4 M NaCl or 4 M KCl, and it is more active in the presence of KCl than in the presence of NaCl. Retains 50% of activity in the presence of 3 M KCl or 2.5 M NaCl.1 Publication

Kineticsi

  1. KM=7.4 mM for ONPG (at 1.9 degrees Celsius and at pH 6.5)1 Publication
  2. KM=4.5 mM for ONPG (at 10 degrees Celsius and at pH 6.5)
  3. KM=5.4 mM for ONPG (at 20 degrees Celsius and at pH 6.5)
  4. KM=5.0 mM for ONPG (at 30 degrees Celsius and at pH 6.5)
  5. KM=4.9 mM for ONPG (at 39 degrees Celsius and at pH 6.5)

Vmax=63 µmol/min/mg enzyme with ONPG as substrate (at 1.9 degrees Celsius and pH 6.5)

Vmax=80 µmol/min/mg enzyme with ONPG as substrate (at 10 degrees Celsius and pH 6.5)

Vmax=223 µmol/min/mg enzyme with ONPG as substrate (at 20 degrees Celsius and pH 6.5)

Vmax=392 µmol/min/mg enzyme with ONPG as substrate (at 30 degrees Celsius and pH 6.5)

Vmax=467 µmol/min/mg enzyme with ONPG as substrate (at 39 degrees Celsius and pH 6.5)

pH dependencei

Optimum pH is 6.5.

Temperature dependencei

Optimum temperature is 42 degrees Celsius. Thermostable at temperatures at or below the optimal temperature for activity, but it is rapidly denatured at temperatures above 42 degrees Celsius. Irreversibly inactivated within 10 minutes at 55 degrees Celsius. Stable during storage at 5 degrees Celsius and loses no activity during storage for 4 months. Retains 10% of activity at 0 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 sitei309 – 3091Nucleophile By similarity
Binding sitei317 – 3171Substrate 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

Enzyme and pathway databases

BRENDAi3.2.1.23. 4880.

Protein family/group databases

CAZyiGH42. Glycoside Hydrolase Family 42.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-galactosidase BgaA (EC:3.2.1.23)
Short name:
Beta-gal
Gene namesi
Name:bgaA
OrganismiPlanococcus sp. (strain 'SOS Orange')
Taxonomic identifieri128803 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPlanococcaceaePlanococcus

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Biotechnological usei

Possible reporter enzyme for halotolerant and halophilic organisms. May also be used in the food industry to digest plant polysaccharides in high-salt processes.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 677677Beta-galactosidase BgaAPRO_0000407692Add
BLAST

Interactioni

Subunit structurei

Dimer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ9KI47.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni357 – 3604Substrate 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.

Q9KI47-1 [UniParc]FASTAAdd to Basket

« Hide

MINDKLPKIW HGGDYNPEQW DSKEIWDEDV RMFKLAGIDV ATLNVFSWAL    50
NQPNEDTYNF DWLDEKINRL YENGIYTCLA TSTAAHPAWM AKKYPDVLRV 100
DFYGRKRKFG SRHNSCPNSP TYRKYSERIA ETLAERYKDH PAVLIWHVSN 150
EYGGYCYCDN CQDAFRNWLS DKYGTLEKLN KAWNTGFWGH TFYEWDEIVA 200
PNMLSEKRED NVSDFQGISL DYRRFQSDRL LDCYKLEYNA IRKHVPTSIP 250
ITTNLMGTYP MLDYFKWAKE MDVVSWDNYP SIDTPFSYTA MTHDLMRGLK 300
GGKPFMLMEQ TPSQQNWQPY NSLKRPGVMR LWSYQAIGRG ADTILYFQLR 350
RSVGACEKYH GAVIEHVGHE HTRVFNEVAQ LGQELNGLSD TLLDARVNAK 400
VAIVFDWENR WATELSSGPS VSLDYVNEVH KYYDALYKLN VQVDMIGVEE 450
DLSKYDVVIA PVLYMVKEGY AAKVEKFVEN GGTFLTTFFS GIVNETDIVT 500
LGGYPGELRK VLGIWAEEID ALHPDETNQI VVKGSRGILS GKYSCNLLFD 550
LIHTEGAEAV AEYGSDFYKG MPVLTVNKFG KGKAWYVASS PDAEFLVDFL 600
QTVCEEAGVE PLLDVPAGVE TTERVKDGQT YLFVLNHNND EVTIELHGSQ 650
YREVLTDEQV SGNLVLKEKG VLILAKV 677
Length:677
Mass (Da):77,484
Last modified:October 1, 2000 - v1
Checksum:i2A1928DADC945E55
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF242542 Genomic DNA. Translation: AAF75984.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF242542 Genomic DNA. Translation: AAF75984.1 .

3D structure databases

ProteinModelPortali Q9KI47.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH42. Glycoside Hydrolase Family 42.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BRENDAi 3.2.1.23. 4880.

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. "Characterization of a salt-tolerant family 42 beta-galactosidase from a psychrophilic antarctic Planococcus isolate."
    Sheridan P.P., Brenchley J.E.
    Appl. Environ. Microbiol. 66:2438-2444(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-8, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, BIOTECHNOLOGY.
    Strain: SOS Orange.

Entry informationi

Entry nameiBGAL_PLASS
AccessioniPrimary (citable) accession number: Q9KI47
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

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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