Reviewed,
UniProtKB/Swiss-Prot P06864 (BGA2_ECOLI)
Last modified
November 3, 2009.
Version 96.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Evolved beta-galactosidase subunit alpha Short name=Beta-gal EC=3.2.1.23 Alternative name(s): Lactase | ||||
| Gene names |
| ||||
| Organism | Escherichia coli (strain K12) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83333 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 1030 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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. |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Glycosidase Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | beta-galactosidase complex Inferred from electronic annotation. Source: InterPro |
| Molecular function | beta-galactosidase activity Inferred from electronic annotation. Source: EC carbohydrate bindingInferred from electronic annotation. Source: InterPro cation bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1030 | 1030 | Evolved beta-galactosidase subunit alpha | PRO_0000057651 | |||||
Sites | |||||||||
| Active site | 449 | 1 | Proton donor Ref.6 | ||||||
| Active site | 512 | 1 | Nucleophile By similarity | ||||||
Natural variations | |||||||||
| Natural variant | 92 | 1 | D → N Improve activity. | ||||||
| Natural variant | 93 | 1 | E → K Improve activity. | ||||||
| Natural variant | 976 | 1 | W → C Improve activity. | ||||||
| Natural variant | 978 | 1 | S → G Improve activity. | ||||||
Experimental info | |||||||||
| Sequence conflict | 275 | 1 | S → T Ref.1 | ||||||
| Sequence conflict | 275 | 1 | S → T Ref.2 | ||||||
| Sequence conflict | 275 | 1 | S → T in AAA57877. Ref.3 | ||||||
| Sequence conflict | 465 | 1 | A → R Ref.1 | ||||||
| Sequence conflict | 465 | 1 | A → R Ref.2 | ||||||
| Sequence conflict | 640 | 1 | T → S Ref.1 | ||||||
| Sequence conflict | 640 | 1 | T → S Ref.2 | ||||||
| Sequence conflict | 649 | 1 | R → P Ref.1 | ||||||
| Sequence conflict | 649 | 1 | R → P Ref.2 | ||||||
| Sequence conflict | 767 | 1 | M → MM Ref.1 | ||||||
| Sequence conflict | 767 | 1 | M → MM Ref.2 | ||||||
| Sequence conflict | 891 – 892 | 2 | ST → QA Ref.1 | ||||||
| Sequence conflict | 891 – 892 | 2 | ST → QA Ref.2 | ||||||
| Sequence conflict | 891 – 892 | 2 | ST → QA in AAA57877. Ref.3 | ||||||
| Sequence conflict | 1026 | 1 | S → T Ref.1 | ||||||
| Sequence conflict | 1026 | 1 | S → T Ref.2 | ||||||
Sequences
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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: 2515108] [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: 3939707] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16397293] [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: 16738553] [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: 6411710] [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: 1540130] [Abstract] Cited for: SUBUNIT. |
Cross-references
Sequence databases | |
|---|---|
| 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. | |
| PIR | GBECE. A65096. |
| RefSeq | AP_003625.1. YP_026199.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1JZ8 based on UniProtKB P00722. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP:2893N. |
| STRING | P06864. |
Protein family/group databases | |
| CAZy | GH2. Glycoside Hydrolase Family 2. |
Genome annotation databases | |
| GeneID | 947583. |
| GenomeReviews | Gene locus JW5511 in contig AP009048_GR. Gene locus b3076 in contig U00096_GR. |
| KEGG | ecj:JW5511. eco:b3076. |
Organism-specific databases | |
| EchoBASE | EB0248. |
| EcoGene | EG10252. ebgA. |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P06864. |
| OMA | KIHALDL. |
Enzyme and pathway databases | |
| BioCyc | EcoCyc:EG10252-MON. |
Gene expression databases | |
| Genevestigator | P06864. |
Family and domain databases | |
| InterPro | IPR014718. Glyco_hydro-type_carb-bd_sub. IPR006101. Glyco_hydro_2. IPR013812. Glyco_hydro_2/20_Ig-like. IPR006104. Glyco_hydro_2_carb-bd. IPR006102. Glyco_hydro_2_Ig-like. IPR006103. Glyco_hydro_2_TIM. IPR004199. Glyco_hydro_42_D5. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view] |
| Gene3D | G3DSA:2.60.40.320. Glyco_hydro_2/20_Ig-like. 2 hits. G3DSA:2.70.98.10. Glyco_hydro_42_D5. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit. |
| Pfam | 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] |
| PRINTS | PR00132. GLHYDRLASE2. |
| PROSITE | PS00719. GLYCOSYL_HYDROL_F2_1. 1 hit. PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| DrugBank | DB00581. Lactulose. |
Entry information
| Entry name | BGA2_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P06864 Secondary accession number(s): P76660, Q2M9D0, Q6BF50 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

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