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P06864 (BGA2_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Evolved beta-galactosidase subunit alpha

Short name=Beta-gal
EC=3.2.1.23
Alternative name(s):
Lactase
Gene names
Name:ebgA
Ordered Locus Names:b3076, JW5511
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length1030 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The wild-type enzyme is an ineffective lactase. Two classes of point mutations dramatically improve activity of the enzyme.

Catalytic activity

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

Subunit structure

Heterooctamer of 4 alpha and 4 beta subunits. Ref.7

Sequence similarities

Belongs to the glycosyl hydrolase 2 family.

Sequence caution

The sequence AAA57877.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentbeta-galactosidase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionbeta-galactosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

carbohydrate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10301030Evolved beta-galactosidase subunit alpha
PRO_0000057651

Sites

Active site4491Proton donor Ref.6
Active site5121Nucleophile By similarity

Natural variations

Natural variant921D → N Improve activity.
Natural variant931E → K Improve activity.
Natural variant9761W → C Improve activity.
Natural variant9781S → G Improve activity.

Experimental info

Sequence conflict2751S → T Ref.1
Sequence conflict2751S → T Ref.2
Sequence conflict2751S → T in AAA57877. Ref.3
Sequence conflict4651A → R Ref.1
Sequence conflict4651A → R Ref.2
Sequence conflict6401T → S Ref.1
Sequence conflict6401T → S Ref.2
Sequence conflict6491R → P Ref.1
Sequence conflict6491R → P Ref.2
Sequence conflict7671M → MM Ref.1
Sequence conflict7671M → MM Ref.2
Sequence conflict891 – 8922ST → QA Ref.1
Sequence conflict891 – 8922ST → QA Ref.2
Sequence conflict891 – 8922ST → QA in AAA57877. Ref.3
Sequence conflict10261S → T Ref.1
Sequence conflict10261S → T Ref.2

Sequences

Sequence LengthMass (Da)Tools
P06864 [UniParc].

Last modified October 11, 2004. Version 4.
Checksum: FEC4D7A558C6EE94

FASTA1,030117,879
        10         20         30         40         50         60 
MNRWENIQLT HENRLAPRAY FFSYDSVAQA RTFARETSSL FLPLSGQWNF HFFDHPLQVP 

        70         80         90        100        110        120 
EAFTSELMAD WGHITVPAMW QMEGHGKLQY TDEGFPFPID VPFVPSDNPT GAYQRIFTLS 

       130        140        150        160        170        180 
DGWQGKQTLI KFDGVETYFE VYVNGQYVGF SKGSRLTAEF DISAMVKTGD NLLCVRVMQW 

       190        200        210        220        230        240 
ADSTYVEDQD MWWSAGIFRD VYLVGKHLTH INDFTVRTDF DEAYCDATLS CEVVLENLAA 

       250        260        270        280        290        300 
SPVVTTLEYT LFDGERVVHS SAIDHLAIEK LTSASFAFTV EQPQQWSAES PYLYHLVMTL 

       310        320        330        340        350        360 
KDANGNVLEV VPQRVGFRDI KVRDGLFWIN NRYVMLHGVN RHDNDHRKGR AVGMDRVEKD 

       370        380        390        400        410        420 
LQLMKQHNIN SVRTAHYPND PRFYELCDIY GLFVMAETDV ESHGFANVGD ISRITDDPQW 

       430        440        450        460        470        480 
EKVYVERIVR HIHAQKNHPS IIIWSLGNES GYGCNIRAMY HAAKALDDTR LVHYEEDRDA 

       490        500        510        520        530        540 
EVVDIISTMY TRVPLMNEFG EYPHPKPRII CEYAHAMGNG PGGLTEYQNV FYKHDCIQGH 

       550        560        570        580        590        600 
YVWEWCDHGI QAQDDHGNVW YKFGGDYGDY PNNYNFCLDG LIYSDQTPGP GLKEYKQVIA 

       610        620        630        640        650        660 
PVKIHARDLT RGELKVENKL WFTTLDDYTL HAEVRAEGET LATQQIKLRD VAPNSEAPLQ 

       670        680        690        700        710        720 
ITLPQLDARE AFLNITVTKD SRTRYSEAGH PIATYQFPLK ENTAQPVPFA PNNARPLTLE 

       730        740        750        760        770        780 
DDRLSCTVRG YNFAITFSKM SGKPTSWQVN GESLLTREPK INFFKPMIDN HKQEYEGLWQ 

       790        800        810        820        830        840 
PNHLQIMQEH LRDFAVEQSD GEVLIISRTV IAPPVFDFGM RCTYIWRIAA DGQVNVALSG 

       850        860        870        880        890        900 
ERYGDYPHII PCIGFTMGIN GEYDQVAYYG RGPGENYADS QQANIIDIWR STVDAMFENY 

       910        920        930        940        950        960 
PFPQNNGNRQ HVRWTALTNR HGNGLLVVPQ RPINFSAWHY TQENIHAAQH CNELQRSDDI 

       970        980        990       1000       1010       1020 
TLNLDHQLLG LGSNSWGSEV LDSWRVWFRD FSYGFTLLPV SGGEATAQSL ASYEFGAGFF 

      1030 
STNLHSENKQ 

« Hide

References

« Hide 'large scale' references
[1]"DNA sequence analysis of artificially evolved ebg enzyme and ebg repressor genes."
Hall B.G., Betts P.W., Wootton J.C.
Genetics 123:635-648(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequence of the ebgA gene of Escherichia coli: comparison with the lacZ gene."
Stokes H.W., Betts P.W., Hall B.G.
Mol. Biol. Evol. 2:469-477(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Escherichia coli K-12: a cooperatively developed annotation snapshot -- 2005."
Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R., Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T., Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H., Thomson N.R., Wishart D., Wanner B.L.
Nucleic Acids Res. 34:1-9(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 275 AND 891-892.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"The active site regions of lacZ and ebg beta-galactosidases are homologous."
Fowler A.V., Smith P.J.
J. Biol. Chem. 258:10204-10207(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE REGIONS.
[7]"The catalytic consequences of experimental evolution. Studies on the subunit structure of the second (ebg) beta-galactosidase of Escherichia coli, and on catalysis by ebgab, an experimental evolvant containing two amino acid substitutions."
Elliott A.C., Sinnott M.L., Smith P.J., Bommuswamy J., Guo Z., Hall B.G., Zhang Y.
Biochem. J. 282:155-164(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64441 Genomic DNA. Translation: AAA61971.1.
X52031 Genomic DNA. Translation: CAA36274.1.
X03228 Genomic DNA. Translation: CAA26977.1. Sequence problems.
U18997 Genomic DNA. Translation: AAA57877.1. Different initiation.
U00096 Genomic DNA. Translation: AAT48164.1.
AP009048 Genomic DNA. Translation: BAE77126.1.
PIRGBECE. A65096.
RefSeqYP_026199.1. NC_000913.3.
YP_491267.1. NC_007779.1.

3D structure databases

ProteinModelPortalP06864.
SMRP06864. Positions 111-470.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-2893N.
IntActP06864. 6 interactions.
STRING511145.b3076.

Chemistry

DrugBankDB00581. Lactulose.

Protein family/group databases

CAZyGH2. Glycoside Hydrolase Family 2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT48164; AAT48164; b3076.
BAE77126; BAE77126; BAE77126.
GeneID12934425.
947583.
KEGGecj:Y75_p3001.
eco:b3076.
PATRIC32121568. VBIEscCol129921_3170.

Organism-specific databases

EchoBASEEB0248.
EcoGeneEG10252. ebgA.

Phylogenomic databases

eggNOGCOG3250.
HOGENOMHOG000252444.
KOK12111.
OMAWENVYVE.
OrthoDBEOG6XWV0T.
PhylomeDBP06864.

Enzyme and pathway databases

BioCycEcoCyc:EG10252-MONOMER.
ECOL316407:JW5511-MONOMER.
SABIO-RKP06864.

Gene expression databases

GenevestigatorP06864.

Family and domain databases

Gene3D2.60.120.260. 1 hit.
2.60.40.320. 2 hits.
2.70.98.10. 1 hit.
3.20.20.80. 1 hit.
InterProIPR004199. B-gal_small/dom_5.
IPR011013. Gal_mutarotase_SF_dom.
IPR008979. Galactose-bd-like.
IPR014718. Glyco_hydro-type_carb-bd_sub.
IPR006101. Glyco_hydro_2.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR023232. Glyco_hydro_2_AS.
IPR023230. Glyco_hydro_2_CS.
IPR006102. Glyco_hydro_2_Ig-like.
IPR006104. Glyco_hydro_2_N.
IPR006103. Glyco_hydro_2_TIM.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF02929. Bgal_small_N. 1 hit.
PF00703. Glyco_hydro_2. 1 hit.
PF02836. Glyco_hydro_2_C. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]
PRINTSPR00132. GLHYDRLASE2.
SMARTSM01038. Bgal_small_N. 1 hit.
[Graphical view]
SUPFAMSSF49303. SSF49303. 2 hits.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF74650. SSF74650. 1 hit.
PROSITEPS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP06864.

Entry information

Entry nameBGA2_ECOLI
AccessionPrimary (citable) accession number: P06864
Secondary accession number(s): P76660, Q2M9D0, Q6BF50
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: October 11, 2004
Last modified: June 11, 2014
This is version 136 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene