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P00722

- BGAL_ECOLI

UniProt

P00722 - BGAL_ECOLI

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Protein

Beta-galactosidase

Gene
lacZ, b0344, JW0335
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.UniRule annotation

Cofactori

Binds 2 magnesium ions per monomer. Can also use manganese.3 Publications
Binds 1 sodium ion per monomer.3 Publications

Enzyme regulationi

Inhibited by phenylethyl thio-beta-D-galactoside (PETG), isopropyl thio-beta-D-galactoside (IPTG), L-ribose, D-galactonolactone, lactose and 2-amino-D-galactose.1 Publication

Kineticsi

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

  1. KM=0.04 mM for p-nitrophenyl beta-D-galactoside6 Publications
  2. KM=0.12 mM for o-nitrophenyl beta-D-galactoside
  3. KM=0.15 mM for 2,3-dinitrophenyl beta-D-galactopyranoside
  4. KM=0.41 mM for 2,5-dinitrophenyl beta-D-galactopyranoside
  5. KM=11.6 mM for p-nitrophenol-alpha-L-arabinopyranoside
  6. KM=16.9 mM for p-nitrophenol-beta-D-fucopyranoside
  7. KM=34 µM for p-nitrophenyl beta-D-galactoside (with magnesium as cofactor and 30 degrees Celsius)
  8. KM=140 µM for o-nitrophenyl beta-D-galactoside (with magnesium as cofactor and 30 degrees Celsius)
  9. KM=940 µM for allolactose (with magnesium as cofactor and 30 degrees Celsius)
  10. 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)

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei103 – 1031Substrate
Metal bindingi202 – 2021Sodium
Binding sitei202 – 2021Substrate
Sitei358 – 3581Transition state stabilizer
Sitei392 – 3921Transition state stabilizer
Metal bindingi417 – 4171Magnesium 1
Metal bindingi419 – 4191Magnesium 1
Active sitei462 – 4621Proton donor2 Publications
Metal bindingi462 – 4621Magnesium 1
Binding sitei462 – 4621Substrate
Active sitei538 – 5381Nucleophile2 Publications
Metal bindingi598 – 5981Magnesium 2
Metal bindingi602 – 6021Sodium; via carbonyl oxygen
Metal bindingi605 – 6051Sodium
Binding sitei605 – 6051Substrate
Binding sitei1000 – 10001Substrate
Sitei1000 – 10001Important for ensuring that an appropriate proportion of lactose is converted to allolactose

GO - Molecular functioni

  1. alkali metal ion binding Source: EcoCyc
  2. beta-galactosidase activity Source: EcoCyc
  3. carbohydrate binding Source: InterPro
  4. magnesium ion binding Source: EcoCyc

GO - Biological processi

  1. lactose catabolic process Source: CACAO
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Magnesium, Manganese, Metal-binding, Sodium

Enzyme and pathway databases

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

Protein family/group databases

CAZyiGH2. Glycoside Hydrolase Family 2.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-galactosidase (EC:3.2.1.23)
Short name:
Beta-gal
Alternative name(s):
Lactase
Gene namesi
Name:lacZ
Ordered Locus Names:b0344, JW0335
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10527. lacZ.

Subcellular locationi

GO - Cellular componenti

  1. beta-galactosidase complex Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi202 – 2021D → 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. 1 Publication
Mutagenesisi202 – 2021D → F: Obliterates all binding and catalysis. 1 Publication
Mutagenesisi358 – 3581H → D, F, L or N: Less stable to heat than wild-type. Causes significant destabilizations of the first transition state. 1 Publication
Mutagenesisi392 – 3921H → E, F or K: Essentially inactive unless very rapid purification. Causes very large destabilizations of the transition state. 1 Publication
Mutagenesisi462 – 4621E → H: Slowly inactivates galactosidase activity by reducing the binding of magnesium. It increases binding specificity. 1 Publication
Mutagenesisi538 – 5381E → Q: 10000-fold decrease in the beta-galactosidase activity. 1 Publication
Mutagenesisi541 – 5411H → E, F or N: Poorly reactive with galactosyl substrates. Less stable to heat than wild-type. 1 Publication
Mutagenesisi602 – 6021F → A: Decreases the stability of the loop 794-804. 1 Publication
Mutagenesisi795 – 7951G → A: It forces the apoenzyme to adopt the closed rather than the open conformation. Reduces the binding affinity. 1 Publication
Mutagenesisi798 – 7981E → A or L: The catalytic efficiency is not increased, when the sodium concentration increases. 1 Publication
Mutagenesisi798 – 7981E → D or Q: Small increase of the catalytic efficiency, when the sodium concentration increases. 1 Publication
Mutagenesisi1000 – 10001W → F, G, L or T: Decreases affinity for substrate. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 10241023Beta-galactosidaseUniRule annotationPRO_0000057650Add
BLAST

Proteomic databases

PRIDEiP00722.

Expressioni

Inductioni

By allolactose.2 Publications

Gene expression databases

GenevestigatoriP00722.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
lacIP030231EBI-369998,EBI-909231
yibFP0ACA11EBI-369998,EBI-1133142

Protein-protein interaction databases

DIPiDIP-10081N.
IntActiP00722. 76 interactions.
STRINGi511145.b0344.

Structurei

Secondary structure

1
1024
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 144
Helixi16 – 183
Beta strandi23 – 264
Beta strandi37 – 393
Helixi40 – 456
Beta strandi52 – 543
Beta strandi57 – 6610
Helixi67 – 693
Helixi73 – 764
Beta strandi83 – 886
Helixi91 – 944
Beta strandi100 – 1056
Beta strandi121 – 13010
Helixi132 – 1365
Beta strandi137 – 1459
Beta strandi147 – 1559
Beta strandi158 – 1647
Beta strandi170 – 1734
Turni175 – 1773
Beta strandi180 – 19112
Helixi194 – 1985
Beta strandi202 – 2054
Beta strandi213 – 2186
Beta strandi220 – 23213
Beta strandi236 – 24914
Beta strandi255 – 2639
Beta strandi266 – 27510
Beta strandi279 – 2813
Beta strandi289 – 29810
Beta strandi304 – 3074
Beta strandi310 – 3189
Turni319 – 3213
Beta strandi323 – 3319
Beta strandi336 – 3394
Beta strandi342 – 3454
Beta strandi352 – 3565
Turni362 – 3643
Helixi370 – 38213
Beta strandi387 – 3893
Helixi397 – 40610
Beta strandi409 – 4135
Beta strandi421 – 4233
Turni424 – 4296
Helixi431 – 4333
Helixi434 – 44815
Beta strandi454 – 4585
Beta strandi461 – 4633
Helixi467 – 47913
Turni489 – 4913
Beta strandi492 – 4943
Beta strandi498 – 5003
Beta strandi514 – 5163
Helixi521 – 5255
Beta strandi534 – 5407
Beta strandi543 – 5453
Helixi550 – 55910
Beta strandi563 – 5697
Beta strandi571 – 5733
Beta strandi576 – 5794
Turni581 – 5833
Beta strandi585 – 5884
Turni590 – 5934
Helixi600 – 6034
Beta strandi607 – 6093
Turni610 – 6123
Helixi617 – 6248
Beta strandi627 – 6337
Beta strandi636 – 6416
Beta strandi652 – 6598
Beta strandi662 – 6709
Beta strandi678 – 6825
Beta strandi691 – 70313
Beta strandi708 – 7103
Beta strandi714 – 72613
Beta strandi740 – 7434
Beta strandi745 – 7528
Beta strandi755 – 7606
Turni761 – 7633
Beta strandi765 – 7717
Beta strandi777 – 7848
Helixi791 – 7944
Beta strandi799 – 8013
Helixi807 – 8148
Turni815 – 8184
Beta strandi820 – 83011
Beta strandi832 – 84514
Beta strandi848 – 86013
Turni861 – 8633
Beta strandi865 – 8739
Beta strandi881 – 89010
Beta strandi894 – 90411
Beta strandi915 – 9228
Helixi923 – 9264
Beta strandi939 – 9479
Beta strandi950 – 96314
Helixi965 – 9706
Helixi974 – 9763
Beta strandi981 – 99111
Beta strandi999 – 10013
Helixi1006 – 10083
Beta strandi1013 – 102210

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP00722.
SMRiP00722. Positions 14-1024.

Miscellaneous databases

EvolutionaryTraceiP00722.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni538 – 5414Substrate bindingUniRule annotation

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000252443.
KOiK01190.
OMAiNPPFVPK.
OrthoDBiEOG6XWV0T.
PhylomeDBiP00722.

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.
HAMAPiMF_01687. Beta_gal.
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.
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]
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00722-1 [UniParc]FASTAAdd to Basket

« Hide

MTMITDSLAV VLQRRDWENP GVTQLNRLAA HPPFASWRNS EEARTDRPSQ     50
QLRSLNGEWR FAWFPAPEAV PESWLECDLP EADTVVVPSN WQMHGYDAPI 100
YTNVTYPITV NPPFVPTENP TGCYSLTFNV DESWLQEGQT RIIFDGVNSA 150
FHLWCNGRWV GYGQDSRLPS EFDLSAFLRA GENRLAVMVL RWSDGSYLED 200
QDMWRMSGIF RDVSLLHKPT TQISDFHVAT RFNDDFSRAV LEAEVQMCGE 250
LRDYLRVTVS LWQGETQVAS GTAPFGGEII DERGGYADRV TLRLNVENPK 300
LWSAEIPNLY RAVVELHTAD GTLIEAEACD VGFREVRIEN GLLLLNGKPL 350
LIRGVNRHEH HPLHGQVMDE QTMVQDILLM KQNNFNAVRC SHYPNHPLWY 400
TLCDRYGLYV VDEANIETHG MVPMNRLTDD PRWLPAMSER VTRMVQRDRN 450
HPSVIIWSLG NESGHGANHD ALYRWIKSVD PSRPVQYEGG GADTTATDII 500
CPMYARVDED QPFPAVPKWS IKKWLSLPGE TRPLILCEYA HAMGNSLGGF 550
AKYWQAFRQY PRLQGGFVWD WVDQSLIKYD ENGNPWSAYG GDFGDTPNDR 600
QFCMNGLVFA DRTPHPALTE AKHQQQFFQF RLSGQTIEVT SEYLFRHSDN 650
ELLHWMVALD GKPLASGEVP LDVAPQGKQL IELPELPQPE SAGQLWLTVR 700
VVQPNATAWS EAGHISAWQQ WRLAENLSVT LPAASHAIPH LTTSEMDFCI 750
ELGNKRWQFN RQSGFLSQMW IGDKKQLLTP LRDQFTRAPL DNDIGVSEAT 800
RIDPNAWVER WKAAGHYQAE AALLQCTADT LADAVLITTA HAWQHQGKTL 850
FISRKTYRID GSGQMAITVD VEVASDTPHP ARIGLNCQLA QVAERVNWLG 900
LGPQENYPDR LTAACFDRWD LPLSDMYTPY VFPSENGLRC GTRELNYGPH 950
QWRGDFQFNI SRYSQQQLME TSHRHLLHAE EGTWLNIDGF HMGIGGDDSW 1000
SPSVSAEFQL SAGRYHYQLV WCQK 1024
Length:1,024
Mass (Da):116,483
Last modified:January 23, 2007 - v2
Checksum:i9D295EF4CEF90B08
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA90981. GBEC.
RefSeqiNP_414878.1. NC_000913.3.
YP_488638.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73447; AAC73447; b0344.
BAE76126; BAE76126; BAE76126.
GeneIDi12934192.
945006.
KEGGiecj:Y75_p0333.
eco:b0344.
PATRICi32115821. VBIEscCol129921_0352.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi A90981. GBEC.
RefSeqi NP_414878.1. NC_000913.3.
YP_488638.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BGL X-ray 2.50 A/B/C/D/E/F/G/H 2-1024 [» ]
1BGM X-ray 2.50 I/J/K/L/M/N/O/P 2-1024 [» ]
1DP0 X-ray 1.70 A/B/C/D 10-1024 [» ]
1F49 X-ray 2.50 A/B/C/D/E/F/G/H 2-1024 [» ]
1F4A X-ray 2.80 A/B/C/D 4-1024 [» ]
1F4H X-ray 2.80 A/B/C/D 4-1024 [» ]
1GHO X-ray 2.50 I/J/K/L/M/N/O/P 2-1024 [» ]
1HN1 X-ray 3.00 A/B/C/D 10-1024 [» ]
1JYN X-ray 1.80 A/B/C/D 10-1024 [» ]
1JYV X-ray 1.75 A/B/C/D 10-1024 [» ]
1JYW X-ray 1.55 A/B/C/D 10-1024 [» ]
1JYX X-ray 1.75 A/B/C/D 10-1024 [» ]
1JYY X-ray 2.70 A/B/C/D/E/F/G/H 2-1024 [» ]
1JYZ X-ray 2.70 I/J/K/L/M/N/O/P 2-1024 [» ]
1JZ0 X-ray 2.60 A/B/C/D/E/F/G/H 2-1024 [» ]
1JZ1 X-ray 2.60 I/J/K/L/M/N/O/P 2-1024 [» ]
1JZ2 X-ray 2.10 A/B/C/D 2-1024 [» ]
1JZ3 X-ray 1.75 A/B/C/D 10-1024 [» ]
1JZ4 X-ray 2.10 A/B/C/D 10-1024 [» ]
1JZ5 X-ray 1.80 A/B/C/D 10-1024 [» ]
1JZ6 X-ray 2.10 A/B/C/D 10-1024 [» ]
1JZ7 X-ray 1.50 A/B/C/D 10-1024 [» ]
1JZ8 X-ray 1.50 A/B/C/D 10-1024 [» ]
1PX3 X-ray 1.60 A/B/C/D 10-1024 [» ]
1PX4 X-ray 1.60 A/B/C/D 10-1024 [» ]
3CZJ X-ray 2.05 A/B/C/D 10-1024 [» ]
3DYM X-ray 2.05 A/B/C/D 10-1024 [» ]
3DYO X-ray 1.80 A/B/C/D 10-1024 [» ]
3DYP X-ray 1.75 A/B/C/D 10-1024 [» ]
3E1F X-ray 3.00 1/2/3/4 10-1024 [» ]
3I3B X-ray 2.20 A/B/C/D 10-1024 [» ]
3I3D X-ray 2.20 A/B/C/D 10-1024 [» ]
3I3E X-ray 2.10 A/B/C/D 10-1024 [» ]
3IAP X-ray 2.00 A/B/C/D 10-1024 [» ]
3IAQ X-ray 2.70 A/B/C/D 10-1024 [» ]
3MUY X-ray 2.50 1/2/3/4 10-1024 [» ]
3MUZ X-ray 1.90 1/2/3/4 10-1024 [» ]
3MV0 X-ray 2.20 1/2/3/4 10-1024 [» ]
3MV1 X-ray 2.20 1/2/3/4 10-1024 [» ]
3SEP X-ray 2.05 A/B/C/D 10-1024 [» ]
3T08 X-ray 2.00 A/B/C/D 10-1024 [» ]
3T09 X-ray 1.75 A/B/C/D 10-1024 [» ]
3T0A X-ray 1.90 A/B/C/D 10-1024 [» ]
3T0B X-ray 2.40 A/B/C/D 10-1024 [» ]
3T0D X-ray 1.93 A/B/C/D 10-1024 [» ]
3T2O X-ray 1.85 A/B/C/D 10-1024 [» ]
3T2P X-ray 2.60 A/B/C/D 10-1024 [» ]
3T2Q X-ray 2.40 A/B/C/D 10-1024 [» ]
3VD3 X-ray 2.80 A/B/C/D 10-1024 [» ]
3VD4 X-ray 2.00 A/B/C/D 10-1024 [» ]
3VD5 X-ray 2.70 A/B/C/D 10-1024 [» ]
3VD7 X-ray 2.87 A/B/C/D 10-1024 [» ]
3VD9 X-ray 2.05 A/B/C/D 10-1024 [» ]
3VDA X-ray 2.50 A/B/C/D 10-1024 [» ]
3VDB X-ray 2.05 A/B/C/D 10-1024 [» ]
3VDC X-ray 2.55 A/B/C/D 10-1024 [» ]
4CKD electron microscopy 13.00 A/B/C/D 1-1024 [» ]
4DUV X-ray 2.10 A/B/C/D 10-1024 [» ]
4DUW X-ray 2.20 A/B/C/D 10-1024 [» ]
4DUX X-ray 2.30 A/B/C/D 10-1024 [» ]
ProteinModelPortali P00722.
SMRi P00722. Positions 14-1024.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10081N.
IntActi P00722. 76 interactions.
STRINGi 511145.b0344.

Chemistry

BindingDBi P00722.
ChEMBLi CHEMBL4603.
DrugBanki DB01093. Dimethyl sulfoxide.

Protein family/group databases

CAZyi GH2. Glycoside Hydrolase Family 2.

Proteomic databases

PRIDEi P00722.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73447 ; AAC73447 ; b0344 .
BAE76126 ; BAE76126 ; BAE76126 .
GeneIDi 12934192.
945006.
KEGGi ecj:Y75_p0333.
eco:b0344.
PATRICi 32115821. VBIEscCol129921_0352.

Organism-specific databases

EchoBASEi EB0522.
EcoGenei EG10527. lacZ.

Phylogenomic databases

HOGENOMi HOG000252443.
KOi K01190.
OMAi NPPFVPK.
OrthoDBi EOG6XWV0T.
PhylomeDBi P00722.

Enzyme and pathway databases

BioCyci EcoCyc:BETAGALACTOSID-MONOMER.
ECOL316407:JW0335-MONOMER.
MetaCyc:BETAGALACTOSID-MONOMER.
SABIO-RK P00722.

Miscellaneous databases

EvolutionaryTracei P00722.
PROi P00722.

Gene expression databases

Genevestigatori P00722.

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.
HAMAPi MF_01687. Beta_gal.
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.
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 ]
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

« Hide 'large scale' publications
  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. 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. 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 SUBSTRATE ANALOGS, 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 SUBSTRATE ANALOGS, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, MUTAGENESIS OF GLY-795.

Entry informationi

Entry nameiBGAL_ECOLI
AccessioniPrimary (citable) accession number: P00722
Secondary accession number(s): Q2MC80
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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