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A1A399

- BGAL_BIFAA

UniProt

A1A399 - BGAL_BIFAA

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Protein

Beta-galactosidase BgaB

Gene

bgaB

Organism
Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Involved in the hydrolysis of transgalactooligosaccharides (TOS). Highly active towards Gal(beta1-4)Gal and Gal(beta1-4)-Gal-containing oligosaccharides. Low activity towards Gal(beta1-3)Gal, lactose and Gal(beta1-3)GalOMe. No activity towards Gal(beta1-6)Gal, Gal(beta1-4)Man, Gal(alpha1-4)Gal, Gal(alpha1-3)Gal(beta1-4)Gal, lactulose, 3'fucosyllactose, lacto-N-fucopentaose I, lacto-N-fucopentaose II, cellobiose, maltose or sucrose. No transglycosylation activity is found at high substrate concentrations (100 mg/ml) and only low transglycosylation activity at lower substrate concentrations (10 mg/ml).2 Publications

Catalytic activityi

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

Enzyme regulationi

Inhibited by high substrate concentrations (100 mg/ml). No effect on activity with various EDTA concentrations (0-1 mM). 20-fold higher activity when cells grown on TOS than when cells grown on galactose, glucose and lactose.2 Publications

Kineticsi

  1. KM=60 mM for Gal(beta1-4)Gal (at 37 degrees Celsius and pH 6.0)2 Publications
  2. KM=2.2 mM for p-nitrophenyl-beta-D-galactopyranoside (PNPG) (at 40 degrees Celsius and pH 6.0)2 Publications
  3. KM=2.2 mM for beta-D-Galp-(1->4)-beta-D-Galp-(1->4)-D-Glcp (at 40 degrees Celsius and pH 6.0)2 Publications
  4. KM=4.0 mM for beta-D-Galp-(1->4)-beta-D-Galp-(1->4)-beta-D-Galp-(1->4)-D-Glcp (at 40 degrees Celsius and pH 6.0)2 Publications
  5. KM=3.7 mM for beta-D-Galp-(1->4)-D-Galp (at 40 degrees Celsius and pH 6.0)2 Publications
  6. KM=6.4 mM for beta-D-Galp-(1->4)-beta-D-Galp-(1->4)-D-Galp (at 40 degrees Celsius and pH 6.0)2 Publications
  7. KM=5.2 mM for beta-D-Galp-(1->4)-beta-D-Galp-(1->4)-beta-D-Galp-(1->4)-D-Galp (at 40 degrees Celsius and pH 6.0)2 Publications

Vmax=1.129 µmol/min/mg enzyme with Gal(beta1-4)Gal as substrate (at 37 degrees Celsius and pH 6.0)2 Publications

pH dependencei

Optimum is pH 6.0 using PNPG or TOS as substrate. Not active below pH 5.2 Publications

Temperature dependencei

Optimum temperature is 50 degrees Celsius using PNPG as substrate (PubMed:15480628). Optimum temperature is 35 degrees Celsius using TOS as substrate (PubMed:10742215). Stable at 40 degrees Celsius. Half-life time at 50 degrees Celsius is 10 minutes.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei122 – 1221SubstrateBy similarity
Binding sitei160 – 1601SubstrateBy similarity
Active sitei161 – 1611Proton donorBy similarity
Active sitei320 – 3201NucleophileBy similarity
Binding sitei328 – 3281SubstrateBy similarity

GO - Molecular functioni

  1. beta-galactosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciBADO367928:GHPT-1457-MONOMER.

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-Gal II
Gene namesi
Name:bgaB
Synonyms:bgaLII
Ordered Locus Names:BAD_1401
OrganismiBifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a)
Taxonomic identifieri367928 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium
ProteomesiUP000008702: Chromosome

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 700699Beta-galactosidase BgaBPRO_0000407683Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Interactioni

Subunit structurei

Trimer (PubMed:15480628). Tetramer (PubMed:10742215).2 Publications

Protein-protein interaction databases

STRINGi367928.BAD_1401.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni368 – 3714Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 42 family.Curated

Phylogenomic databases

eggNOGiCOG1874.
HOGENOMiHOG000117811.
KOiK12308.
OrthoDBiEOG6GTZGG.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
3.40.50.880. 1 hit.
InterProiIPR013738. 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.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

A1A399-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSARRNFEWP ELLTADGRGI AFGGDYNPDQ WSEDIWDDDI RLMKQAGVNT
60 70 80 90 100
VALAIFSWDR IQPTEDRWDF GWLDRIIDKL GNAGIVVDLA SATATAPLWL
110 120 130 140 150
YESHPEVLPR DKYGHPVNAG SRQSWSPTSP VFKEYALTLC RKLAERYGTN
160 170 180 190 200
PYVTAWHMGN EYGWNNREDY SDNALEAFRA WCRRKYGTID ALNQAWGTTF
210 220 230 240 250
WGQEMNGFDE VLIPRFMGAD SMVNPGQKLD FERFGNDMLL DFYKAERDAI
260 270 280 290 300
AEICPDKPFT TNFMVSTDQC CMDYAAWAKE VNFVSNDHYF HEGESHLDEL
310 320 330 340 350
ACSDALMDSL ALGKPWYVME HSTSAVQWKP LNTRKRKGET VRDSLAHVAM
360 370 380 390 400
GADAINFFQW RASAFGAEAF HSAMVPHAGE DTKLFRQVCE LGASLHTLAD
410 420 430 440 450
AGVQGTELAH SDTAILFSAE SEWATRSQTL PSMKLNHWHD VRDWYRAFLD
460 470 480 490 500
AGSRADIVPL AYDWSSYKTV VLPTVLILSA ADTQRLADFA AAGGRVVVGY
510 520 530 540 550
ATGLIDEHFH TWLGGYPGAG DGLLRSMLGV RGEEFNILGA EAEGEPGEIR
560 570 580 590 600
LSSADDSAAL DGTTTRLWQN DVNVTGEHAQ VLATYAGEEA DEWELDGTAA
610 620 630 640 650
VTRNPYGSGE AYFVGCDLDV ADLTKLVRAY LAASSQENAD VLHTVRASAD
660 670 680 690 700
ATFDFYLPRG KKTVELQGIE GEPVILFQTD REEKPGSYTV RRNGVLVVRR
Length:700
Mass (Da):78,025
Last modified:May 3, 2011 - v2
Checksum:i9EDB064761188A52
GO

Sequence cautioni

The sequence BAF40182.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti213 – 23018IPRFM…GQKLD → HPTVHGRRLRWSTPARSST in AAR24113. (PubMed:15480628)CuratedAdd
BLAST
Sequence conflicti536 – 5361N → T in AAR24113. (PubMed:15480628)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY359872 Genomic DNA. Translation: AAR24113.1.
AP009256 Genomic DNA. Translation: BAF40182.1. Different initiation.
RefSeqiYP_910264.1. NC_008618.1.

Genome annotation databases

EnsemblBacteriaiBAF40182; BAF40182; BAD_1401.
GeneIDi4557550.
KEGGibad:BAD_1401.
PATRICi21102249. VBIBifAdo27973_1479.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY359872 Genomic DNA. Translation: AAR24113.1 .
AP009256 Genomic DNA. Translation: BAF40182.1 . Different initiation.
RefSeqi YP_910264.1. NC_008618.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 367928.BAD_1401.

Protein family/group databases

CAZyi GH42. Glycoside Hydrolase Family 42.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAF40182 ; BAF40182 ; BAD_1401 .
GeneIDi 4557550.
KEGGi bad:BAD_1401.
PATRICi 21102249. VBIBifAdo27973_1479.

Phylogenomic databases

eggNOGi COG1874.
HOGENOMi HOG000117811.
KOi K12308.
OrthoDBi EOG6GTZGG.

Enzyme and pathway databases

BioCyci BADO367928:GHPT-1457-MONOMER.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
3.40.50.880. 1 hit.
InterProi 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.
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

« Hide 'large scale' publications
  1. "beta-galactosidase from Bifidobacterium adolescentis DSM20083 prefers beta(1,4)-galactosides over lactose."
    Hinz S.W., van den Brock L.A., Beldman G., Vincken J.P., Voragen A.G.
    Appl. Microbiol. Biotechnol. 66:276-284(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-16; 20-29; 455-463 AND 535-546, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY.
    Strain: ATCC 15703 / DSM 20083 / NCTC 11814 / E194a.
  2. "Bifidobacterium adolescentis complete genome sequence."
    Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S., Tanaka K., Watanabe K.
    Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15703 / DSM 20083 / NCTC 11814 / E194a.
  3. "Characterization of a novel beta-galactosidase from Bifidobacterium adolescentis DSM 20083 active towards transgalactooligosaccharides."
    Van Laere K.M., Abee T., Schols H.A., Beldman G., Voragen A.G.
    Appl. Environ. Microbiol. 66:1379-1384(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    Strain: ATCC 15703 / DSM 20083 / NCTC 11814 / E194a.

Entry informationi

Entry nameiBGAL_BIFAA
AccessioniPrimary (citable) accession number: A1A399
Secondary accession number(s): Q5J883
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: May 3, 2011
Last modified: October 1, 2014
This is version 43 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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