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P06864

- BGA2_ECOLI

UniProt

P06864 - BGA2_ECOLI

Protein

Evolved beta-galactosidase subunit alpha

Gene

ebgA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 4 (11 Oct 2004)
      Previous versions | rss
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    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 – 5121NucleophileBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    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

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10301030Evolved beta-galactosidase subunit alphaPRO_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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 2 family.Curated

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti275 – 2751S → T(PubMed:2515108)Curated
    Sequence conflicti275 – 2751S → T(PubMed:3939707)Curated
    Sequence conflicti275 – 2751S → T in AAA57877. (PubMed:9278503)Curated
    Sequence conflicti465 – 4651A → R(PubMed:2515108)Curated
    Sequence conflicti465 – 4651A → R(PubMed:3939707)Curated
    Sequence conflicti640 – 6401T → S(PubMed:2515108)Curated
    Sequence conflicti640 – 6401T → S(PubMed:3939707)Curated
    Sequence conflicti649 – 6491R → P(PubMed:2515108)Curated
    Sequence conflicti649 – 6491R → P(PubMed:3939707)Curated
    Sequence conflicti767 – 7671M → MM(PubMed:2515108)Curated
    Sequence conflicti767 – 7671M → MM(PubMed:3939707)Curated
    Sequence conflicti891 – 8922ST → QA(PubMed:2515108)Curated
    Sequence conflicti891 – 8922ST → QA(PubMed:3939707)Curated
    Sequence conflicti891 – 8922ST → QA in AAA57877. (PubMed:9278503)Curated
    Sequence conflicti1026 – 10261S → T(PubMed:2515108)Curated
    Sequence conflicti1026 – 10261S → T(PubMed:3939707)Curated

    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 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...
    MobiDBi 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

    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: October 1, 2014
    This is version 137 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