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P19668

- BGAL_GEOKU

UniProt

P19668 - BGAL_GEOKU

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Protein

Beta-galactosidase bgaB

Gene
bgaB
Organism
Geobacillus kaustophilus
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Hydrolyzes 6-bromo-2-naphthyl-beta-D-galactopyranoside and o-nitrophenyl-beta-D-galactopyranoside (ONPG). Possesses a high level of transgalactosylation activity. Hydrolyzes lactose in milk.1 Publication

Catalytic activityi

Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.2 Publications

Enzyme regulationi

By divalent metal ions. Fe2+, Zn2+, Cu2+, Pb2+ and Sn2+ inhibit 52, 76.6, 85.3, 100 and 100% of the enzyme activity, respectively. Other metal cations and EDTA do not inhibit this enzyme. Thiol reagents 2-mercaptoethanol and dithiothreitol have no effect on the activity. Sulfhydryl group-blocking reagents p-chloromercuribenzoic acid and iodoacetic acid inhibit 86.2 and 74% of the enzyme activity, respectively.1 Publication

Kineticsi

  1. KM=2.96 mM for ONPG (at 55 degrees Celsius and pH 7.0)2 Publications

Vmax=6.62 µmol/min/mg enzyme with ONPG as substrate (at 55 degrees Celsius and pH 7.0)

pH dependencei

Optimum pH is 7.0. Retains more than 80% of the activity at a pH range of 6.0-7.5.

Temperature dependencei

Optimum temperature for the activity is 70 degrees Celsius using ONPG as substrate. Stable up to 70 degrees Celsius (1 Publication). Retains 80% of the activity at 75 degrees Celsius (1 Publication). Kinetics of thermal inactivation and half-life times at 60, 65 and 70 degrees Celsius are 120, 50 and 9 hours, respectively.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei109 – 1091Substrate By similarity
Metal bindingi113 – 1131Zinc By similarity
Binding sitei147 – 1471Substrate By similarity
Active sitei148 – 1481Proton donor By similarity
Metal bindingi156 – 1561Zinc By similarity
Metal bindingi158 – 1581Zinc By similarity
Metal bindingi161 – 1611Zinc By similarity
Active sitei303 – 3031Nucleophile By similarity
Binding sitei311 – 3111Substrate 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 bgaB (EC:3.2.1.23)
Short name:
Beta-gal
Alternative name(s):
Beta-galactosidase I
Lactase
Gene namesi
Name:bgaB
OrganismiGeobacillus kaustophilus
Taxonomic identifieri1462 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Biotechnological usei

Has potential for enzyme application in low-lactose milk production during milk pasteurization.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 672672Beta-galactosidase bgaBPRO_0000057691Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP19668.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni351 – 3544Substrate 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.

P19668-1 [UniParc]FASTAAdd to Basket

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MNVLSSICYG GDYNPEQWPE EIWYEDAKLM QKAGVNLVSL GIFSWSKIEP    50
SDGVFDFEWL DKVIDILYDH GVYINLGTAT ATTPAWFVKK YPDSLPIDES 100
GVILSFGSRQ HYCPNHPQLI THIKRLVRAI AERYKNHPAL KMWHVNNEYA 150
CHVSKCFCEN CAVAFRKWLK ERYKTIDELN ERWGTNFWGQ RYNHWDEINP 200
PRKAPTFINP SQELDYYRFM NDSILKLFLT EKEILREVTP DIPVSTNFMG 250
SFKPLNYFQW AQHVDIVTWD SYPDPREGLP IQHAMMNDLM RSLRKGQPFI 300
LMEQVTSHVN WRDINVPKPP GVMRLWSYAT IARGADGIMF FQWRQSRAGA 350
EKFHGAMVPH FLNENNRIYR EVTQLGQELK KLDCLVGSRI KAEVAIIFDW 400
ENWWAVELSS KPHNKLRYIP IVEAYYRELY KRNIAVDFVR PSDDLTKYKV 450
VIAPMLYMVK EGEDENLRQF VANGGTLIVS FFSGIVDEND RVHLGGYPGP 500
LRDILGIFVE EFVPYPETKV NKIYSNDGEY DCTTWADIIR LEGAEPLATF 550
KGDWYAGLPA VTRNCYGKGE GIYVGTYPDS NYLGRLLEQV FAKHHINPIL 600
EVAENVEVQQ RETDEWKYLI IINHNDYEVT LSLPEDKIYQ NMIDGKCFRG 650
GELRIQGVDV AVLREHDEAG KV 672
Length:672
Mass (Da):78,053
Last modified:February 1, 1991 - v1
Checksum:iFF611FFBEF68F09A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M13466 Genomic DNA. Translation: AAA22262.1.
PIRiA29836.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M13466 Genomic DNA. Translation: AAA22262.1 .
PIRi A29836.

3D structure databases

ProteinModelPortali P19668.
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. "Structure of a beta-galactosidase gene of Bacillus stearothermophilus."
    Hirata H., Fukazawa T., Negoro S., Okada H.
    J. Bacteriol. 166:722-727(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: ATCC 8005 / DSM 7263 / JCM 20319 / NCIMB 8547 / NRRL NRS-81 / IAM 11001.
  2. "Molecular basis of isozyme formation of beta-galactosidases in Bacillus stearothermophilus: isolation of two beta-galactosidase genes, bgaA and bgaB."
    Hirata H., Negoro S., Okada H.
    J. Bacteriol. 160:9-14(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
    Strain: ATCC 8005 / DSM 7263 / JCM 20319 / NCIMB 8547 / NRRL NRS-81 / IAM 11001.
  3. "Production, purification, and characterization of a potential thermostable galactosidase for milk lactose hydrolysis from Bacillus stearothermophilus."
    Chen W., Chen H., Xia Y., Zhao J., Tian F., Zhang H.
    J. Dairy Sci. 91:1751-1758(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, BIOTECHNOLOGY.
    Strain: ATCC 8005 / DSM 7263 / JCM 20319 / NCIMB 8547 / NRRL NRS-81 / IAM 11001.

Entry informationi

Entry nameiBGAL_GEOKU
AccessioniPrimary (citable) accession number: P19668
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: June 11, 2014
This is version 74 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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