P00722 (BGAL_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	1024 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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)

Ontologies

Keywords
Ligand	Magnesium Manganese Metal-binding Sodium
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	lactose catabolic process Inferred from mutant phenotype PubMed 14022758. Source: EcoCyc
Cellular_component	beta-galactosidase complex Inferred from direct assay PubMed 14304855Ref.22. Source: EcoCyc
Molecular_function	alkali metal ion binding Inferred from direct assay Ref.24PubMed 4860414. Source: EcoCyc beta-galactosidase activity Inferred from direct assay PubMed 14304855. Source: EcoCyc carbohydrate binding Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from direct assay Ref.23PubMed 4625429. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
lacI	P03023	1	EBI-369998,EBI-909231
yibF	P0ACA1	1	EBI-369998,EBI-1133142

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 1024

1023

Beta-galactosidase HAMAP-Rule MF_01687

PRO_0000057650

Regions

Region

538 – 541

4

Substrate binding HAMAP-Rule MF_01687

Sites

Active site

462

1

Proton donor Ref.10 Ref.11

Active site

538

1

Nucleophile Ref.10 Ref.12

Metal binding

202

1

Sodium

Metal binding

417

1

Magnesium 1

Metal binding

419

1

Magnesium 1

Metal binding

462

1

Magnesium 1

Metal binding

598

1

Magnesium 2

Metal binding

602

1

Sodium; via carbonyl oxygen

Metal binding

605

1

Sodium

Binding site

103

1

Substrate

Binding site

202

1

Substrate

Binding site

462

1

Substrate

Binding site

605

1

Substrate

Binding site

1000

1

Substrate

Site

358

1

Transition state stabilizer

Site

392

1

Transition state stabilizer

Site

1000

1

Important for ensuring that an appropriate proportion of lactose is converted to allolactose

Experimental info

Mutagenesis

202

1

D → 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

Mutagenesis

202

1

D → F: Obliterates all binding and catalysis. Ref.19

Mutagenesis

358

1

H → D, F, L or N: Less stable to heat than wild-type. Causes significant destabilizations of the first transition state. Ref.16

Mutagenesis

392

1

H → E, F or K: Essentially inactive unless very rapid purification. Causes very large destabilizations of the transition state. Ref.17

Mutagenesis

462

1

E → H: Slowly inactivates galactosidase activity by reducing the binding of magnesium. It increases binding specificity. Ref.13

Mutagenesis

538

1

E → Q: 10000-fold decrease in the beta-galactosidase activity. Ref.24

Mutagenesis

541

1

H → E, F or N: Poorly reactive with galactosyl substrates. Less stable to heat than wild-type. Ref.14

Mutagenesis

602

1

F → A: Decreases the stability of the loop 794-804. Ref.24

Mutagenesis

795

1

G → A: It forces the apoenzyme to adopt the closed rather than the open conformation. Reduces the binding affinity. Ref.25

Mutagenesis

798

1

E → A or L: The catalytic efficiency is not increased, when the sodium concentration increases. Ref.21

Mutagenesis

798

1

E → D or Q: Small increase of the catalytic efficiency, when the sodium concentration increases. Ref.21

Mutagenesis

1000

1

W → F, G, L or T: Decreases affinity for substrate. Ref.18

Secondary structure

1

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1024

Helix Strand Turn

Details...

Helix

11 – 14

4

Helix

16 – 18

3

Beta strand

23 – 26

4

Beta strand

37 – 39

3

Helix

40 – 45

6

Beta strand

52 – 54

3

Beta strand

57 – 66

10

Helix

67 – 69

3

Helix

73 – 76

4

Beta strand

83 – 88

6

Helix

91 – 94

4

Beta strand

100 – 105

6

Beta strand

121 – 130

10

Helix

132 – 136

5

Beta strand

137 – 145

9

Beta strand

147 – 155

9

Beta strand

158 – 164

7

Beta strand

170 – 173

4

Turn

175 – 177

3

Beta strand

180 – 191

12

Helix

194 – 198

5

Beta strand

202 – 205

4

Beta strand

213 – 218

6

Beta strand

220 – 232

13

Beta strand

236 – 249

14

Beta strand

255 – 263

9

Beta strand

266 – 275

10

Beta strand

279 – 281

3

Beta strand

289 – 298

10

Beta strand

304 – 307

4

Beta strand

310 – 318

9

Turn

319 – 321

3

Beta strand

323 – 331

9

Beta strand

336 – 339

4

Beta strand

342 – 345

4

Beta strand

352 – 356

5

Turn

362 – 364

3

Helix

370 – 382

13

Beta strand

387 – 389

3

Helix

397 – 406

10

Beta strand

409 – 413

5

Beta strand

421 – 423

3

Turn

424 – 429

6

Helix

431 – 433

3

Helix

434 – 448

15

Beta strand

454 – 458

5

Beta strand

461 – 463

3

Helix

467 – 479

13

Turn

489 – 491

3

Beta strand

492 – 494

3

Beta strand

498 – 500

3

Beta strand

514 – 516

3

Helix

521 – 525

5

Beta strand

534 – 540

7

Beta strand

543 – 545

3

Helix

550 – 559

10

Beta strand

563 – 569

7

Beta strand

571 – 573

3

Beta strand

576 – 579

4

Turn

581 – 583

3

Beta strand

585 – 588

4

Turn

590 – 593

4

Helix

600 – 603

4

Beta strand

607 – 609

3

Turn

610 – 612

3

Helix

617 – 624

8

Beta strand

627 – 633

7

Beta strand

636 – 641

6

Beta strand

652 – 659

8

Beta strand

662 – 670

9

Beta strand

678 – 682

5

Beta strand

691 – 703

13

Beta strand

708 – 710

3

Beta strand

714 – 726

13

Beta strand

740 – 743

4

Beta strand

745 – 752

8

Beta strand

755 – 760

6

Turn

761 – 763

3

Beta strand

765 – 771

7

Beta strand

777 – 784

8

Helix

791 – 794

4

Beta strand

799 – 801

3

Helix

807 – 814

8

Turn

815 – 818

4

Beta strand

820 – 830

11

Beta strand

832 – 845

14

Beta strand

848 – 860

13

Turn

861 – 863

3

Beta strand

865 – 873

9

Beta strand

881 – 890

10

Beta strand

894 – 904

11

Beta strand

915 – 922

8

Helix

923 – 926

4

Beta strand

939 – 947

9

Beta strand

950 – 963

14

Helix

965 – 970

6

Helix

974 – 976

3

Beta strand

981 – 991

11

Beta strand

999 – 1001

3

Helix

1006 – 1008

3

Beta strand

1013 – 1022

10

Sequences

	Sequence		Length	Mass (Da)
	P00722 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 9D295EF4CEF90B08	FASTA	1,024	116,483
	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

References

	« Hide 'large scale' referencesShow '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 277:1453-1474(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.

Web resources

Worthington enzyme manual

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.

PIR

GBEC. A90981.

RefSeq

NP_414878.1. NC_000913.2.
YP_488638.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	10-1023	[»]
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	[»]

ProteinModelPortal

P00722.

SMR

P00722. Positions 14-1024.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00722. 76 interactions.

STRING

511145.b0344.

Protein family/group databases

CAZy

GH2. Glycoside Hydrolase Family 2.

Proteomic databases

PRIDE

P00722.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73447; AAC73447; b0344.
BAE76126; BAE76126; BAE76126.

GeneID

12934192.
945006.

KEGG

ecj:Y75_p0333.
eco:b0344.

PATRIC

32115821. VBIEscCol129921_0352.

Organism-specific databases

EchoBASE

EB0522.

EcoGene

EG10527. lacZ.

Phylogenomic databases

HOGENOM

HOG000252443.

KO

K01190.

OMA

DFHVATH.

ProtClustDB

PRK09525.

Enzyme and pathway databases

BioCyc

EcoCyc:BETAGALACTOSID-MONOMER.
ECOL316407:JW0335-MONOMER.
MetaCyc:BETAGALACTOSID-MONOMER.

SABIO-RK

P00722.

Gene expression databases

Genevestigator

P00722.

Family and domain databases

Gene3D

2.60.40.320. 2 hits.
2.70.98.10. 1 hit.
3.20.20.80. 1 hit.

HAMAP

MF_01687. Beta_gal.

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.
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]

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

BindingDB

P00722.

ChEMBL

CHEMBL4603.

DrugBank

DB01093. Dimethyl sulfoxide.

EvolutionaryTrace

P00722.

Entry information

Entry name

BGAL_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 147 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program