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P00722

- BGAL_ECOLI

UniProt

P00722 - BGAL_ECOLI

Protein

Beta-galactosidase

Gene

lacZ

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

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

    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-galactoside6 Publications
    3. KM=0.15 mM for 2,3-dinitrophenyl beta-D-galactopyranoside6 Publications
    4. KM=0.41 mM for 2,5-dinitrophenyl beta-D-galactopyranoside6 Publications
    5. KM=11.6 mM for p-nitrophenol-alpha-L-arabinopyranoside6 Publications
    6. KM=16.9 mM for p-nitrophenol-beta-D-fucopyranoside6 Publications
    7. KM=34 µM for p-nitrophenyl beta-D-galactoside (with magnesium as cofactor and 30 degrees Celsius)6 Publications
    8. KM=140 µM for o-nitrophenyl beta-D-galactoside (with magnesium as cofactor and 30 degrees Celsius)6 Publications
    9. KM=940 µM for allolactose (with magnesium as cofactor and 30 degrees Celsius)6 Publications
    10. KM=1350 µM for lactose (with magnesium as cofactor and 30 degrees Celsius)6 Publications

    Vmax=30.9 µmol/min/mg enzyme with lactose as substrate (with magnesium as cofactor and 30 degrees Celsius)6 Publications

    Vmax=49.7 µmol/min/mg enzyme with allolactose as substrate (with magnesium as cofactor and 30 degrees Celsius)6 Publications

    Vmax=59.7 µmol/min/mg enzyme with p-nitrophenyl beta-D-galactoside as substrate (with magnesium as cofactor and 30 degrees Celsius)6 Publications

    Vmax=360 µmol/min/mg enzyme with o-nitrophenyl beta-D-galactoside as substrate (with magnesium as cofactor and 30 degrees Celsius)6 Publications

    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 11 Publication
    Metal bindingi419 – 4191Magnesium 11 Publication
    Active sitei462 – 4621Proton donor2 Publications
    Metal bindingi462 – 4621Magnesium 11 Publication
    Binding sitei462 – 4621Substrate
    Active sitei538 – 5381Nucleophile2 Publications
    Metal bindingi598 – 5981Magnesium 21 Publication
    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

    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

    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-galactosidasePRO_0000057650Add
    BLAST

    Proteomic databases

    PRIDEiP00722.

    Expressioni

    Inductioni

    By allolactose.1 Publication

    Gene expression databases

    GenevestigatoriP00722.

    Interactioni

    Subunit structurei

    Homotetramer.4 Publications

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00722.

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 2 family.Curated

    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

    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: October 1, 2014
    This is version 160 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