Evolved beta-galactosidase subunit alpha - Escherichia coli (strain K12)

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P06864 (BGA2_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 125. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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

Name:	ebgA
Ordered Locus Names:	b3076, JW5511

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	1030 AA.
Sequence status	Complete.
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.
Sequence caution	The sequence AAA57877.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome Reference 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 binding Inferred 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

Proton donor Ref.6

Active site

512

Nucleophile By similarity

Natural variations

Natural variant

D → N Improve activity.

Natural variant

E → K Improve activity.

Natural variant

976

W → C Improve activity.

Natural variant

978

S → G Improve activity.

Experimental info

Sequence conflict

275

S → T Ref.1

Sequence conflict

275

S → T Ref.2

Sequence conflict

275

S → T in AAA57877. Ref.3

Sequence conflict

465

A → R Ref.1

Sequence conflict

465

A → R Ref.2

Sequence conflict

640

T → S Ref.1

Sequence conflict

640

T → S Ref.2

Sequence conflict

649

R → P Ref.1

Sequence conflict

649

R → P Ref.2

Sequence conflict

767

M → MM Ref.1

Sequence conflict

767

M → MM Ref.2

Sequence conflict

891 – 892

ST → QA Ref.1

Sequence conflict

891 – 892

ST → QA Ref.2

Sequence conflict

891 – 892

ST → QA in AAA57877. Ref.3

Sequence conflict

1026

S → T Ref.1

Sequence conflict

1026

S → T Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P06864 [UniParc].

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

1,030

117,879

        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' referencesShow '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 277:1453-1474(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.

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.
PIR	GBECE. A65096.
RefSeq	YP_026199.1. NC_000913.2. YP_491267.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P06864.
SMR	P06864. Positions 111-470.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2893N.
IntAct	P06864. 1 interaction.
STRING	511145.b3076.
Protein family/group databases
CAZy	GH2. Glycoside Hydrolase Family 2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAT48164; AAT48164; b3076. BAE77126; BAE77126; BAE77126.
GeneID	12934425. 947583.
KEGG	ecj:Y75_p3001. eco:b3076.
PATRIC	32121568. VBIEscCol129921_3170.
Organism-specific databases
EchoBASE	EB0248.
EcoGene	EG10252. ebgA.
Phylogenomic databases
eggNOG	COG3250.
HOGENOM	HOG000252444.
KO	K12111.
OMA	PMNRWEN.
ProtClustDB	PRK10340.
Enzyme and pathway databases
BioCyc	EcoCyc:EG10252-MONOMER. ECOL316407:JW5511-MONOMER.
SABIO-RK	P06864.
Gene expression databases
Genevestigator	P06864.
Family and domain databases
Gene3D	2.60.40.320. 2 hits. 2.70.98.10. 1 hit. 3.20.20.80. 1 hit.
InterPro	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]
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.
SMART	SM01038. Bgal_small_N. 1 hit. [Graphical view]
SUPFAM	SSF49785. Gal_bind_like. 1 hit. SSF74650. Gal_mut_like. 1 hit. SSF49303. Glyco_hydro_2Ig. 2 hits. SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00719. GLYCOSYL_HYDROL_F2_1. 1 hit. PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00581. Lactulose.

Entry information

Entry name

BGA2_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 125 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Escherichia coli

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents