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P06864

- BGA2_ECOLI

UniProt

P06864 - BGA2_ECOLI

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Protein
Evolved beta-galactosidase subunit alpha
Gene
ebgA, b3076, JW5511
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei449 – 4491Proton donor1 Publication
Active sitei512 – 5121Nucleophile By similarity

GO - Molecular functioni

  1. beta-galactosidase activity Source: UniProtKB-EC
  2. carbohydrate binding Source: InterPro
Complete GO annotation...

GO - Biological processi

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

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

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

Protein family/group databases

CAZyiGH2. Glycoside Hydrolase Family 2.

Names & Taxonomyi

Protein namesi
Recommended name:
Evolved beta-galactosidase subunit alpha (EC:3.2.1.23)
Short name:
Beta-gal
Alternative name(s):
Lactase
Gene namesi
Name:ebgA
Ordered Locus Names:b3076, JW5511
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10252. ebgA.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10301030Evolved beta-galactosidase subunit alpha
PRO_0000057651Add
BLAST

Expressioni

Gene expression databases

GenevestigatoriP06864.

Interactioni

Subunit structurei

Heterooctamer of 4 alpha and 4 beta subunits.1 Publication

Protein-protein interaction databases

DIPiDIP-2893N.
IntActiP06864. 6 interactions.
STRINGi511145.b3076.

Structurei

3D structure databases

ProteinModelPortaliP06864.
SMRiP06864. Positions 111-470.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3250.
HOGENOMiHOG000252444.
KOiK12111.
OMAiWENVYVE.
OrthoDBiEOG6XWV0T.
PhylomeDBiP06864.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
2.60.40.320. 2 hits.
2.70.98.10. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR004199. 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]
PfamiPF02929. 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]
PRINTSiPR00132. GLHYDRLASE2.
SMARTiSM01038. Bgal_small_N. 1 hit.
[Graphical view]
SUPFAMiSSF49303. SSF49303. 2 hits.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF74650. SSF74650. 1 hit.
PROSITEiPS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P06864-1 [UniParc]FASTAAdd to Basket

« Hide

MNRWENIQLT HENRLAPRAY FFSYDSVAQA RTFARETSSL FLPLSGQWNF     50
HFFDHPLQVP EAFTSELMAD WGHITVPAMW QMEGHGKLQY TDEGFPFPID 100
VPFVPSDNPT GAYQRIFTLS DGWQGKQTLI KFDGVETYFE VYVNGQYVGF 150
SKGSRLTAEF DISAMVKTGD NLLCVRVMQW ADSTYVEDQD MWWSAGIFRD 200
VYLVGKHLTH INDFTVRTDF DEAYCDATLS CEVVLENLAA SPVVTTLEYT 250
LFDGERVVHS SAIDHLAIEK LTSASFAFTV EQPQQWSAES PYLYHLVMTL 300
KDANGNVLEV VPQRVGFRDI KVRDGLFWIN NRYVMLHGVN RHDNDHRKGR 350
AVGMDRVEKD LQLMKQHNIN SVRTAHYPND PRFYELCDIY GLFVMAETDV 400
ESHGFANVGD ISRITDDPQW EKVYVERIVR HIHAQKNHPS IIIWSLGNES 450
GYGCNIRAMY HAAKALDDTR LVHYEEDRDA EVVDIISTMY TRVPLMNEFG 500
EYPHPKPRII CEYAHAMGNG PGGLTEYQNV FYKHDCIQGH YVWEWCDHGI 550
QAQDDHGNVW YKFGGDYGDY PNNYNFCLDG LIYSDQTPGP GLKEYKQVIA 600
PVKIHARDLT RGELKVENKL WFTTLDDYTL HAEVRAEGET LATQQIKLRD 650
VAPNSEAPLQ ITLPQLDARE AFLNITVTKD SRTRYSEAGH PIATYQFPLK 700
ENTAQPVPFA PNNARPLTLE DDRLSCTVRG YNFAITFSKM SGKPTSWQVN 750
GESLLTREPK INFFKPMIDN HKQEYEGLWQ PNHLQIMQEH LRDFAVEQSD 800
GEVLIISRTV IAPPVFDFGM RCTYIWRIAA DGQVNVALSG ERYGDYPHII 850
PCIGFTMGIN GEYDQVAYYG RGPGENYADS QQANIIDIWR STVDAMFENY 900
PFPQNNGNRQ HVRWTALTNR HGNGLLVVPQ RPINFSAWHY TQENIHAAQH 950
CNELQRSDDI TLNLDHQLLG LGSNSWGSEV LDSWRVWFRD FSYGFTLLPV 1000
SGGEATAQSL ASYEFGAGFF STNLHSENKQ 1030
Length:1,030
Mass (Da):117,879
Last modified:October 11, 2004 - v4
Checksum:iFEC4D7A558C6EE94
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti92 – 921D → N Improve activity.
Natural varianti93 – 931E → K Improve activity.
Natural varianti976 – 9761W → C Improve activity.
Natural varianti978 – 9781S → G Improve activity.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti275 – 2751S → T1 Publication
Sequence conflicti275 – 2751S → T1 Publication
Sequence conflicti275 – 2751S → T in AAA57877. 1 Publication
Sequence conflicti465 – 4651A → R1 Publication
Sequence conflicti465 – 4651A → R1 Publication
Sequence conflicti640 – 6401T → S1 Publication
Sequence conflicti640 – 6401T → S1 Publication
Sequence conflicti649 – 6491R → P1 Publication
Sequence conflicti649 – 6491R → P1 Publication
Sequence conflicti767 – 7671M → MM1 Publication
Sequence conflicti767 – 7671M → MM1 Publication
Sequence conflicti891 – 8922ST → QA1 Publication
Sequence conflicti891 – 8922ST → QA1 Publication
Sequence conflicti891 – 8922ST → QA in AAA57877. 1 Publication
Sequence conflicti1026 – 10261S → T1 Publication
Sequence conflicti1026 – 10261S → T1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA65096. GBECE.
RefSeqiYP_026199.1. NC_000913.3.
YP_491267.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAT48164; AAT48164; b3076.
BAE77126; BAE77126; BAE77126.
GeneIDi12934425.
947583.
KEGGiecj:Y75_p3001.
eco:b3076.
PATRICi32121568. VBIEscCol129921_3170.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi A65096. GBECE.
RefSeqi YP_026199.1. NC_000913.3.
YP_491267.1. NC_007779.1.

3D structure databases

ProteinModelPortali P06864.
SMRi P06864. Positions 111-470.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-2893N.
IntActi P06864. 6 interactions.
STRINGi 511145.b3076.

Chemistry

DrugBanki DB00581. Lactulose.

Protein family/group databases

CAZyi GH2. Glycoside Hydrolase Family 2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAT48164 ; AAT48164 ; b3076 .
BAE77126 ; BAE77126 ; BAE77126 .
GeneIDi 12934425.
947583.
KEGGi ecj:Y75_p3001.
eco:b3076.
PATRICi 32121568. VBIEscCol129921_3170.

Organism-specific databases

EchoBASEi EB0248.
EcoGenei EG10252. ebgA.

Phylogenomic databases

eggNOGi COG3250.
HOGENOMi HOG000252444.
KOi K12111.
OMAi WENVYVE.
OrthoDBi EOG6XWV0T.
PhylomeDBi P06864.

Enzyme and pathway databases

BioCyci EcoCyc:EG10252-MONOMER.
ECOL316407:JW5511-MONOMER.
SABIO-RK P06864.

Miscellaneous databases

PROi P06864.

Gene expression databases

Genevestigatori P06864.

Family and domain databases

Gene3Di 2.60.120.260. 1 hit.
2.60.40.320. 2 hits.
2.70.98.10. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR004199. 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 ]
Pfami PF02929. 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 ]
PRINTSi PR00132. GLHYDRLASE2.
SMARTi SM01038. Bgal_small_N. 1 hit.
[Graphical view ]
SUPFAMi SSF49303. SSF49303. 2 hits.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF74650. SSF74650. 1 hit.
PROSITEi PS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. 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.

Entry informationi

Entry nameiBGA2_ECOLI
AccessioniPrimary (citable) accession number: P06864
Secondary accession number(s): P76660, Q2M9D0, Q6BF50
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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