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Protein

Evolved beta-galactosidase subunit alpha

Gene

ebgA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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 – 5121NucleophileBy similarity

GO - Molecular functioni

  1. beta-galactosidase activity Source: UniProtKB-EC
  2. carbohydrate binding Source: InterPro
  3. hydrolase activity, hydrolyzing O-glycosyl compounds Source: GO_Central

GO - Biological processi

  1. carbohydrate metabolic process Source: GO_Central
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
  2. intracellular membrane-bounded organelle Source: GO_Central
Complete GO annotation...

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.
InParanoidiP06864.
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

        10         20         30         40         50
MNRWENIQLT HENRLAPRAY FFSYDSVAQA RTFARETSSL FLPLSGQWNF
60 70 80 90 100
HFFDHPLQVP EAFTSELMAD WGHITVPAMW QMEGHGKLQY TDEGFPFPID
110 120 130 140 150
VPFVPSDNPT GAYQRIFTLS DGWQGKQTLI KFDGVETYFE VYVNGQYVGF
160 170 180 190 200
SKGSRLTAEF DISAMVKTGD NLLCVRVMQW ADSTYVEDQD MWWSAGIFRD
210 220 230 240 250
VYLVGKHLTH INDFTVRTDF DEAYCDATLS CEVVLENLAA SPVVTTLEYT
260 270 280 290 300
LFDGERVVHS SAIDHLAIEK LTSASFAFTV EQPQQWSAES PYLYHLVMTL
310 320 330 340 350
KDANGNVLEV VPQRVGFRDI KVRDGLFWIN NRYVMLHGVN RHDNDHRKGR
360 370 380 390 400
AVGMDRVEKD LQLMKQHNIN SVRTAHYPND PRFYELCDIY GLFVMAETDV
410 420 430 440 450
ESHGFANVGD ISRITDDPQW EKVYVERIVR HIHAQKNHPS IIIWSLGNES
460 470 480 490 500
GYGCNIRAMY HAAKALDDTR LVHYEEDRDA EVVDIISTMY TRVPLMNEFG
510 520 530 540 550
EYPHPKPRII CEYAHAMGNG PGGLTEYQNV FYKHDCIQGH YVWEWCDHGI
560 570 580 590 600
QAQDDHGNVW YKFGGDYGDY PNNYNFCLDG LIYSDQTPGP GLKEYKQVIA
610 620 630 640 650
PVKIHARDLT RGELKVENKL WFTTLDDYTL HAEVRAEGET LATQQIKLRD
660 670 680 690 700
VAPNSEAPLQ ITLPQLDARE AFLNITVTKD SRTRYSEAGH PIATYQFPLK
710 720 730 740 750
ENTAQPVPFA PNNARPLTLE DDRLSCTVRG YNFAITFSKM SGKPTSWQVN
760 770 780 790 800
GESLLTREPK INFFKPMIDN HKQEYEGLWQ PNHLQIMQEH LRDFAVEQSD
810 820 830 840 850
GEVLIISRTV IAPPVFDFGM RCTYIWRIAA DGQVNVALSG ERYGDYPHII
860 870 880 890 900
PCIGFTMGIN GEYDQVAYYG RGPGENYADS QQANIIDIWR STVDAMFENY
910 920 930 940 950
PFPQNNGNRQ HVRWTALTNR HGNGLLVVPQ RPINFSAWHY TQENIHAAQH
960 970 980 990 1000
CNELQRSDDI TLNLDHQLLG LGSNSWGSEV LDSWRVWFRD FSYGFTLLPV
1010 1020 1030
SGGEATAQSL ASYEFGAGFF STNLHSENKQ
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP06864.
SMRiP06864. Positions 111-470.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

DrugBankiDB00581. Lactulose.

Protein family/group databases

CAZyiGH2. Glycoside Hydrolase Family 2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EchoBASEiEB0248.
EcoGeneiEG10252. ebgA.

Phylogenomic databases

eggNOGiCOG3250.
HOGENOMiHOG000252444.
InParanoidiP06864.
KOiK12111.
OMAiWENVYVE.
OrthoDBiEOG6XWV0T.
PhylomeDBiP06864.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP06864.

Gene expression databases

GenevestigatoriP06864.

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]
ProtoNetiSearch...

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: February 4, 2015
This is version 140 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.