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P00722 (BGAL_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-galactosidase

Short name=Beta-gal
EC=3.2.1.23
Alternative name(s):
Lactase
Gene names
Name:lacZ
Ordered Locus Names:b0344, JW0335
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length1024 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. HAMAP-Rule MF_01687

Cofactor

Binds 2 magnesium ions per monomer. Can also use manganese. Ref.9 Ref.13 Ref.21

Binds 1 sodium ion per monomer. Ref.9 Ref.13 Ref.21

Enzyme regulation

Inhibited by phenylethyl thio-beta-D-galactoside (PETG), isopropyl thio-beta-D-galactoside (IPTG), L-ribose, D-galactonolactone, lactose and 2-amino-D-galactose. Ref.25

Subunit structure

Homotetramer. Ref.22

Induction

By allolactose. Ref.8 Ref.25

Sequence similarities

Belongs to the glycosyl hydrolase 2 family.

Biophysicochemical properties

Kinetic parameters:

The values for the enzymatic assays using manganese as cofactor are very close.

KM=0.04 mM for p-nitrophenyl beta-D-galactoside Ref.9 Ref.14 Ref.16 Ref.18 Ref.19 Ref.25

KM=0.12 mM for o-nitrophenyl beta-D-galactoside

KM=0.15 mM for 2,3-dinitrophenyl beta-D-galactopyranoside

KM=0.41 mM for 2,5-dinitrophenyl beta-D-galactopyranoside

KM=11.6 mM for p-nitrophenol-alpha-L-arabinopyranoside

KM=16.9 mM for p-nitrophenol-beta-D-fucopyranoside

KM=34 µM for p-nitrophenyl beta-D-galactoside (with magnesium as cofactor and 30 degrees Celsius)

KM=140 µM for o-nitrophenyl beta-D-galactoside (with magnesium as cofactor and 30 degrees Celsius)

KM=940 µM for allolactose (with magnesium as cofactor and 30 degrees Celsius)

KM=1350 µM for lactose (with magnesium as cofactor and 30 degrees Celsius)

Vmax=30.9 µmol/min/mg enzyme with lactose as substrate (with magnesium as cofactor and 30 degrees Celsius)

Vmax=49.7 µmol/min/mg enzyme with allolactose as substrate (with magnesium as cofactor and 30 degrees Celsius)

Vmax=59.7 µmol/min/mg enzyme with p-nitrophenyl beta-D-galactoside as substrate (with magnesium as cofactor and 30 degrees Celsius)

Vmax=360 µmol/min/mg enzyme with o-nitrophenyl beta-D-galactoside as substrate (with magnesium as cofactor and 30 degrees Celsius)

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 10241023Beta-galactosidase HAMAP-Rule MF_01687
PRO_0000057650

Regions

Region538 – 5414Substrate binding HAMAP-Rule MF_01687

Sites

Active site4621Proton donor Ref.10 Ref.11
Active site5381Nucleophile Ref.10 Ref.12
Metal binding2021Sodium
Metal binding4171Magnesium 1
Metal binding4191Magnesium 1
Metal binding4621Magnesium 1
Metal binding5981Magnesium 2
Metal binding6021Sodium; via carbonyl oxygen
Metal binding6051Sodium
Binding site1031Substrate
Binding site2021Substrate
Binding site4621Substrate
Binding site6051Substrate
Binding site10001Substrate
Site3581Transition state stabilizer
Site3921Transition state stabilizer
Site10001Important for ensuring that an appropriate proportion of lactose is converted to allolactose

Experimental info

Mutagenesis2021D → E or N: Causes a significant decrease in binding affinity in the absence of monovalent cations or in the presence of potassium ions, but only a moderate decrease in the presence of sodium ions. Ref.19
Mutagenesis2021D → F: Obliterates all binding and catalysis. Ref.19
Mutagenesis3581H → D, F, L or N: Less stable to heat than wild-type. Causes significant destabilizations of the first transition state. Ref.16
Mutagenesis3921H → E, F or K: Essentially inactive unless very rapid purification. Causes very large destabilizations of the transition state. Ref.17
Mutagenesis4621E → H: Slowly inactivates galactosidase activity by reducing the binding of magnesium. It increases binding specificity. Ref.13
Mutagenesis5381E → Q: 10000-fold decrease in the beta-galactosidase activity. Ref.24
Mutagenesis5411H → E, F or N: Poorly reactive with galactosyl substrates. Less stable to heat than wild-type. Ref.14
Mutagenesis6021F → A: Decreases the stability of the loop 794-804. Ref.24
Mutagenesis7951G → A: It forces the apoenzyme to adopt the closed rather than the open conformation. Reduces the binding affinity. Ref.25
Mutagenesis7981E → A or L: The catalytic efficiency is not increased, when the sodium concentration increases. Ref.21
Mutagenesis7981E → D or Q: Small increase of the catalytic efficiency, when the sodium concentration increases. Ref.21
Mutagenesis10001W → F, G, L or T: Decreases affinity for substrate. Ref.18

Secondary structure

............................................................................................................................................................................................... 1024
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00722 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 9D295EF4CEF90B08

FASTA1,024116,483
        10         20         30         40         50         60 
MTMITDSLAV VLQRRDWENP GVTQLNRLAA HPPFASWRNS EEARTDRPSQ QLRSLNGEWR 

        70         80         90        100        110        120 
FAWFPAPEAV PESWLECDLP EADTVVVPSN WQMHGYDAPI YTNVTYPITV NPPFVPTENP 

       130        140        150        160        170        180 
TGCYSLTFNV DESWLQEGQT RIIFDGVNSA FHLWCNGRWV GYGQDSRLPS EFDLSAFLRA 

       190        200        210        220        230        240 
GENRLAVMVL RWSDGSYLED QDMWRMSGIF RDVSLLHKPT TQISDFHVAT RFNDDFSRAV 

       250        260        270        280        290        300 
LEAEVQMCGE LRDYLRVTVS LWQGETQVAS GTAPFGGEII DERGGYADRV TLRLNVENPK 

       310        320        330        340        350        360 
LWSAEIPNLY RAVVELHTAD GTLIEAEACD VGFREVRIEN GLLLLNGKPL LIRGVNRHEH 

       370        380        390        400        410        420 
HPLHGQVMDE QTMVQDILLM KQNNFNAVRC SHYPNHPLWY TLCDRYGLYV VDEANIETHG 

       430        440        450        460        470        480 
MVPMNRLTDD PRWLPAMSER VTRMVQRDRN HPSVIIWSLG NESGHGANHD ALYRWIKSVD 

       490        500        510        520        530        540 
PSRPVQYEGG GADTTATDII CPMYARVDED QPFPAVPKWS IKKWLSLPGE TRPLILCEYA 

       550        560        570        580        590        600 
HAMGNSLGGF AKYWQAFRQY PRLQGGFVWD WVDQSLIKYD ENGNPWSAYG GDFGDTPNDR 

       610        620        630        640        650        660 
QFCMNGLVFA DRTPHPALTE AKHQQQFFQF RLSGQTIEVT SEYLFRHSDN ELLHWMVALD 

       670        680        690        700        710        720 
GKPLASGEVP LDVAPQGKQL IELPELPQPE SAGQLWLTVR VVQPNATAWS EAGHISAWQQ 

       730        740        750        760        770        780 
WRLAENLSVT LPAASHAIPH LTTSEMDFCI ELGNKRWQFN RQSGFLSQMW IGDKKQLLTP 

       790        800        810        820        830        840 
LRDQFTRAPL DNDIGVSEAT RIDPNAWVER WKAAGHYQAE AALLQCTADT LADAVLITTA 

       850        860        870        880        890        900 
HAWQHQGKTL FISRKTYRID GSGQMAITVD VEVASDTPHP ARIGLNCQLA QVAERVNWLG 

       910        920        930        940        950        960 
LGPQENYPDR LTAACFDRWD LPLSDMYTPY VFPSENGLRC GTRELNYGPH QWRGDFQFNI 

       970        980        990       1000       1010       1020 
SRYSQQQLME TSHRHLLHAE EGTWLNIDGF HMGIGGDDSW SPSVSAEFQL SAGRYHYQLV 


WCQK 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of the lacZ gene of Escherichia coli."
Kalnins A., Otto K., Ruether U., Mueller-Hill B.
EMBO J. 2:593-597(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[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 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"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.
[5]"Amino acid sequence of beta-galactosidase. XI. Peptide ordering procedures and the complete sequence."
Fowler A.V., Zabin I.
J. Biol. Chem. 253:5521-5525(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-1024.
[6]"Molecular consequences of deletion formation mediated by the transposon Tn9."
Calos M.P., Miller J.H.
Nature 285:38-41(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 356-476.
[7]"Sequence of the lactose permease gene."
Buechel D.E., Gronenborn B., Mueller-Hill B.
Nature 283:541-545(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1008-1024.
[8]"lac repressor-operator interaction. VI. The natural inducer of the lac operon."
Jobe A., Bourgeois S.
J. Mol. Biol. 69:397-408(1972) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY ALLOLACTOSE.
[9]"Interaction of divalent cations with beta-galactosidase (Escherichia coli)."
Huber R.E., Parfett C., Woulfe-Flanagan H., Thompson D.J.
Biochemistry 18:4090-4095(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
[10]"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.
[11]"Identification of an essential carboxylate group at the active site of lacZ beta-galactosidase from Escherichia coli."
Herrchen M., Legler G.
Eur. J. Biochem. 138:527-531(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE GLU-462.
[12]"Glu-537, not Glu-461, is the nucleophile in the active site of (lac Z) beta-galactosidase from Escherichia coli."
Gebler J.C., Aebersold R., Withers S.G.
J. Biol. Chem. 267:11126-11130(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE GLU-538.
[13]"E461H-beta-galactosidase (Escherichia coli): altered divalent metal specificity and slow but reversible metal inactivation."
Martinez-Bilbao M., Gaunt M.T., Huber R.E.
Biochemistry 34:13437-13442(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLU-462, COFACTOR.
[14]"The beta-galactosidase (Escherichia coli) reaction is partly facilitated by interactions of His-540 with the C6 hydroxyl of galactose."
Roth N.J., Huber R.E.
J. Biol. Chem. 271:14296-14301(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-541.
[15]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[16]"His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and helps to mediate catalysis."
Roth N.J., Rob B., Huber R.E.
Biochemistry 37:10099-10107(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-358.
[17]"His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition state."
Huber R.E., Hlede I.Y., Roth N.J., McKenzie K.C., Ghumman K.K.
Biochem. Cell Biol. 79:183-193(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-392.
[18]"Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for binding, catalysis, and synthesis of allolactose, the natural lac operon inducer."
Huber R.E., Hakda S., Cheng C., Cupples C.G., Edwards R.A.
Biochemistry 42:1796-1803(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TRP-1000.
[19]"A study of the relationships of interactions between Asp-201, Na+ or K+, and galactosyl C6 hydroxyl and their effects on binding and reactivity of beta-galactosidase."
Xu J., McRae M.A., Harron S., Rob B., Huber R.E.
Biochem. Cell Biol. 82:275-284(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-202.
[20]"The structure of E. coli beta-galactosidase."
Matthews B.W.
C. R. Biol. 328:549-556(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[21]"Beta-galactosidase (Escherichia coli) has a second catalytically important Mg2+ site."
Sutendra G., Wong S., Fraser M.E., Huber R.E.
Biochem. Biophys. Res. Commun. 352:566-570(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: COFACTOR, MUTAGENESIS OF GLU-798.
[22]"Three-dimensional structure of beta-galactosidase from E. coli."
Jacobson R.H., Zhang X.-J., Dubose R.F., Matthews B.W.
Nature 369:761-766(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, SUBUNIT.
[23]"High resolution refinement of beta-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for alpha-complementation."
Juers D.H., Jacobson R.H., Wigley D., Zhang X.-J., Huber R.E., Tronrud D.E., Matthews B.W.
Protein Sci. 9:1685-1699(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND SODIUM IONS.
[24]"A structural view of the action of Escherichia coli (lacZ) beta-galactosidase."
Juers D.H., Heightman T.D., Vasella A., McCarter J.D., Mackenzie L., Withers S.G., Matthews B.W.
Biochemistry 40:14781-14794(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH ANALOGS SUBSTRATE, MUTAGENESIS OF GLU-538 AND PHE-602, REACTION MECHANISM.
[25]"Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase."
Juers D.H., Hakda S., Matthews B.W., Huber R.E.
Biochemistry 42:13505-13511(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 10-1024 OF MUTANT ALA-795 IN COMPLEX WITH MAGNESIUM IONS, SODIUM IONS AND ANALOGS SUBSTRATE, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, MUTAGENESIS OF GLY-795.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J01636 Genomic DNA. Translation: AAA24053.1.
V00296 Genomic DNA. Translation: CAA23573.1.
U73857 Genomic DNA. Translation: AAB18068.1.
U00096 Genomic DNA. Translation: AAC73447.1.
AP009048 Genomic DNA. Translation: BAE76126.1.
V00295 Genomic DNA. Translation: CAA23570.1.
PIRGBEC. A90981.
RefSeqNP_414878.1. NC_000913.3.
YP_488638.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BGLX-ray2.50A/B/C/D/E/F/G/H2-1024[»]
1BGMX-ray2.50I/J/K/L/M/N/O/P2-1024[»]
1DP0X-ray1.70A/B/C/D10-1024[»]
1F49X-ray2.50A/B/C/D/E/F/G/H2-1024[»]
1F4AX-ray2.80A/B/C/D4-1024[»]
1F4HX-ray2.80A/B/C/D4-1024[»]
1GHOX-ray2.50I/J/K/L/M/N/O/P2-1024[»]
1HN1X-ray3.00A/B/C/D10-1024[»]
1JYNX-ray1.80A/B/C/D10-1024[»]
1JYVX-ray1.75A/B/C/D10-1024[»]
1JYWX-ray1.55A/B/C/D10-1024[»]
1JYXX-ray1.75A/B/C/D10-1024[»]
1JYYX-ray2.70A/B/C/D/E/F/G/H2-1024[»]
1JYZX-ray2.70I/J/K/L/M/N/O/P2-1024[»]
1JZ0X-ray2.60A/B/C/D/E/F/G/H2-1024[»]
1JZ1X-ray2.60I/J/K/L/M/N/O/P2-1024[»]
1JZ2X-ray2.10A/B/C/D2-1024[»]
1JZ3X-ray1.75A/B/C/D10-1024[»]
1JZ4X-ray2.10A/B/C/D10-1024[»]
1JZ5X-ray1.80A/B/C/D10-1024[»]
1JZ6X-ray2.10A/B/C/D10-1024[»]
1JZ7X-ray1.50A/B/C/D10-1024[»]
1JZ8X-ray1.50A/B/C/D10-1024[»]
1PX3X-ray1.60A/B/C/D10-1024[»]
1PX4X-ray1.60A/B/C/D10-1024[»]
3CZJX-ray2.05A/B/C/D10-1024[»]
3DYMX-ray2.05A/B/C/D10-1024[»]
3DYOX-ray1.80A/B/C/D10-1024[»]
3DYPX-ray1.75A/B/C/D10-1024[»]
3E1FX-ray3.001/2/3/410-1024[»]
3I3BX-ray2.20A/B/C/D10-1024[»]
3I3DX-ray2.20A/B/C/D10-1024[»]
3I3EX-ray2.10A/B/C/D10-1024[»]
3IAPX-ray2.00A/B/C/D10-1024[»]
3IAQX-ray2.70A/B/C/D10-1024[»]
3MUYX-ray2.501/2/3/410-1024[»]
3MUZX-ray1.901/2/3/410-1024[»]
3MV0X-ray2.201/2/3/410-1024[»]
3MV1X-ray2.201/2/3/410-1024[»]
3SEPX-ray2.05A/B/C/D10-1024[»]
3T08X-ray2.00A/B/C/D10-1024[»]
3T09X-ray1.75A/B/C/D10-1024[»]
3T0AX-ray1.90A/B/C/D10-1024[»]
3T0BX-ray2.40A/B/C/D10-1024[»]
3T0DX-ray1.93A/B/C/D10-1024[»]
3T2OX-ray1.85A/B/C/D10-1024[»]
3T2PX-ray2.60A/B/C/D10-1024[»]
3T2QX-ray2.40A/B/C/D10-1024[»]
3VD3X-ray2.80A/B/C/D10-1024[»]
3VD4X-ray2.00A/B/C/D10-1024[»]
3VD5X-ray2.70A/B/C/D10-1024[»]
3VD7X-ray2.87A/B/C/D10-1024[»]
3VD9X-ray2.05A/B/C/D10-1024[»]
3VDAX-ray2.50A/B/C/D10-1024[»]
3VDBX-ray2.05A/B/C/D10-1024[»]
3VDCX-ray2.55A/B/C/D10-1024[»]
4CKDelectron microscopy13.00A/B/C/D1-1024[»]
4DUVX-ray2.10A/B/C/D10-1024[»]
4DUWX-ray2.20A/B/C/D10-1024[»]
4DUXX-ray2.30A/B/C/D10-1024[»]
ProteinModelPortalP00722.
SMRP00722. Positions 14-1024.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10081N.
IntActP00722. 76 interactions.
STRING511145.b0344.

Chemistry

BindingDBP00722.
ChEMBLCHEMBL4603.
DrugBankDB01093. Dimethyl sulfoxide.

Protein family/group databases

CAZyGH2. Glycoside Hydrolase Family 2.

Proteomic databases

PRIDEP00722.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73447; AAC73447; b0344.
BAE76126; BAE76126; BAE76126.
GeneID12934192.
945006.
KEGGecj:Y75_p0333.
eco:b0344.
PATRIC32115821. VBIEscCol129921_0352.

Organism-specific databases

EchoBASEEB0522.
EcoGeneEG10527. lacZ.

Phylogenomic databases

HOGENOMHOG000252443.
KOK01190.
OMANPPFVPK.
OrthoDBEOG6XWV0T.
PhylomeDBP00722.

Enzyme and pathway databases

BioCycEcoCyc:BETAGALACTOSID-MONOMER.
ECOL316407:JW0335-MONOMER.
MetaCyc:BETAGALACTOSID-MONOMER.
SABIO-RKP00722.

Gene expression databases

GenevestigatorP00722.

Family and domain databases

Gene3D2.60.120.260. 1 hit.
2.60.40.320. 2 hits.
2.70.98.10. 1 hit.
3.20.20.80. 1 hit.
HAMAPMF_01687. Beta_gal.
InterProIPR004199. 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.
IPR023933. Glyco_hydro_2_beta_Galsidase.
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]
PfamPF02929. 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]
PRINTSPR00132. GLHYDRLASE2.
SMARTSM01038. Bgal_small_N. 1 hit.
[Graphical view]
SUPFAMSSF49303. SSF49303. 2 hits.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF74650. SSF74650. 1 hit.
PROSITEPS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
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EvolutionaryTraceP00722.
PROP00722.

Entry information

Entry nameBGAL_ECOLI
AccessionPrimary (citable) accession number: P00722
Secondary accession number(s): Q2MC80
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Escherichia coli

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