ECOLI:BGAL

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	lacZ
Protein Name(s)	Beta-galactosidase Beta-gal Lactase
External Links
UniProt	P00722
EMBL	J01636 V00296 U73857 U00096 AP009048 V00295
PIR	A90981
RefSeq	NP_414878.1 YP_488638.1
PDB	1BGL 1BGM 1DP0 1F49 1F4A 1F4H 1GHO 1HN1 1JYN 1JYV 1JYW 1JYX 1JYY 1JYZ 1JZ0 1JZ1 1JZ2 1JZ3 1JZ4 1JZ5 1JZ6 1JZ7 1JZ8 1PX3 1PX4 3CZJ 3DYM 3DYO 3DYP 3E1F 3I3B 3I3D 3I3E 3IAP 3IAQ 3J7H 3MUY 3MUZ 3MV0 3MV1 3SEP 3T08 3T09 3T0A 3T0B 3T0D 3T2O 3T2P 3T2Q 3VD3 3VD4 3VD5 3VD7 3VD9 3VDA 3VDB 3VDC 4CKD 4DUV 4DUW 4DUX
PDBsum	1BGL 1BGM 1DP0 1F49 1F4A 1F4H 1GHO 1HN1 1JYN 1JYV 1JYW 1JYX 1JYY 1JYZ 1JZ0 1JZ1 1JZ2 1JZ3 1JZ4 1JZ5 1JZ6 1JZ7 1JZ8 1PX3 1PX4 3CZJ 3DYM 3DYO 3DYP 3E1F 3I3B 3I3D 3I3E 3IAP 3IAQ 3J7H 3MUY 3MUZ 3MV0 3MV1 3SEP 3T08 3T09 3T0A 3T0B 3T0D 3T2O 3T2P 3T2Q 3VD3 3VD4 3VD5 3VD7 3VD9 3VDA 3VDB 3VDC 4CKD 4DUV 4DUW 4DUX
ProteinModelPortal	P00722
SMR	P00722
DIP	DIP-10081N
IntAct	P00722
STRING	511145.b0344
BindingDB	P00722
ChEMBL	CHEMBL4603
CAZy	GH2
PRIDE	P00722
EnsemblBacteria	AAC73447 BAE76126
GeneID	12934192 945006
KEGG	ecj:Y75_p0333 eco:b0344
PATRIC	32115821
EchoBASE	EB0522
EcoGene	EG10527
HOGENOM	HOG000252443
InParanoid	P00722
KO	K01190
OMA	TNRHEHH
OrthoDB	EOG6XWV0T
PhylomeDB	P00722
BioCyc	EcoCyc:BETAGALACTOSID-MONOMER ECOL316407:JW0335-MONOMER MetaCyc:BETAGALACTOSID-MONOMER
SABIO-RK	P00722
EvolutionaryTrace	P00722
PRO	PR:P00722
Proteomes	UP000000318 UP000000625
Genevestigator	P00722
GO	GO:0009341 GO:0031420 GO:0004565 GO:0030246 GO:0000287 GO:0005990
Gene3D	2.60.120.260 2.60.40.320 2.70.98.10 3.20.20.80
HAMAP	MF_01687
InterPro	IPR004199 IPR011013 IPR008979 IPR014718 IPR006101 IPR013812 IPR023232 IPR023933 IPR023230 IPR006102 IPR006104 IPR006103 IPR013781 IPR017853
Pfam	PF02929 PF00703 PF02836 PF02837
PRINTS	PR00132
SMART	SM01038
SUPFAM	SSF49303 SSF49785 SSF51445 SSF74650
PROSITE	PS00719 PS00608

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0005990	lactose catabolic process	PMID:22475386^[1]	ECO:0000315			P	Table 1	complete CACAO 4355
involved_in	GO:0005990	lactose catabolic process	PMID:22475386^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0009341	beta-galactosidase complex	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10527 PANTHER:PTN001600393	C	Seeded From UniProt	complete
involved_in	GO:0005990	lactose catabolic process	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10527 PANTHER:PTN001600393	P	Seeded From UniProt	complete
enables	GO:0004565	beta-galactosidase activity	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10527 PANTHER:PTN001600393	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:25953817^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00722	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:24613486^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00722	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:23850452^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00722	F	Seeded From UniProt	complete
enables	GO:0031420	alkali metal ion binding	PMID:4860414^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0031420	alkali metal ion binding	PMID:11732897^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0009341	beta-galactosidase complex	PMID:8008071^[8]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0009341	beta-galactosidase complex	PMID:14304855^[9]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0005990	lactose catabolic process	PMID:14022758^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004565	beta-galactosidase activity	PMID:14304855^[9]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	PMID:4625429^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	PMID:11045615^[12]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR011013	F	Seeded From UniProt	complete
enables	GO:0004553	hydrolase activity, hydrolyzing O-glycosyl compounds	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006101 InterPro:IPR006102 InterPro:IPR006103 InterPro:IPR006104	F	Seeded From UniProt	complete
enables	GO:0004565	beta-galactosidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004199	F	Seeded From UniProt	complete
involved_in	GO:0005975	carbohydrate metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004199 InterPro:IPR006101 InterPro:IPR006102 InterPro:IPR006103 InterPro:IPR006104 InterPro:IPR011013	P	Seeded From UniProt	complete
part_of	GO:0009341	beta-galactosidase complex	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004199	C	Seeded From UniProt	complete
enables	GO:0016798	hydrolase activity, acting on glycosyl bonds	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR023933	F	Seeded From UniProt	complete
enables	GO:0030246	carbohydrate binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR011013 InterPro:IPR014718	F	Seeded From UniProt	complete
enables	GO:0004565	beta-galactosidase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.2.1.23	F	Seeded From UniProt	complete
enables	GO:0016798	hydrolase activity, acting on glycosyl bonds	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000084121	F	Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000084121	F	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
enables	GO:0016798	hydrolase activity, acting on glycosyl bonds	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0326	F	Seeded From UniProt	complete
involved_in	GO:0008152	metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0326	P	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Craig, DB et al. (2012) Random mutagenesis suggests that sequence errors are not a major cause of variation in the activity of individual molecules of β-galactosidase. Biochem. Cell Biol. 90 540-7 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Bartesaghi, A et al. (2015) 2.2 Å resolution cryo-EM structure of β-galactosidase in complex with a cell-permeant inhibitor. Science 348 1147-51 PubMed GONUTS page
↑ Vinothkumar, KR et al. (2014) Molecular mechanism of antibody-mediated activation of β-galactosidase. Structure 22 621-7 PubMed GONUTS page
↑ Hall, Z et al. (2013) The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. Structure 21 1325-37 PubMed GONUTS page
↑ Neville, MC & Ling, GN (1967) Synergistic activation of beta-galactosidase by Na and Cs. Arch. Biochem. Biophys. 118 596-610 PubMed GONUTS page
↑ Juers, DH et al. (2001) A structural view of the action of Escherichia coli (lacZ) beta-galactosidase. Biochemistry 40 14781-94 PubMed GONUTS page
↑ Jacobson, RH et al. (1994) Three-dimensional structure of beta-galactosidase from E. coli. Nature 369 761-6 PubMed GONUTS page
↑ ^9.0 ^9.1 CRAVEN, GR et al. (1965) PURIFICATION, COMPOSITION, AND MOLECULAR WEIGHT OF THE BETA-GALACTOSIDASE OF ESCHERICHIA COLI K12. J. Biol. Chem. 240 2468-77 PubMed GONUTS page
↑ COOK, A & LEDERBERG, J (1962) Recombination studies of lactose nonfermenting mutants of Escherichia coli K-12. Genetics 47 1335-53 PubMed GONUTS page
↑ Tenu, JP et al. (1972) Kinetic study of the activation process of -galactosidase from Escherichia coli by Mg 2+ . Eur. J. Biochem. 26 112-8 PubMed GONUTS page
↑ Juers, DH et al. (2000) High resolution refinement of beta-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for alpha-complementation. Protein Sci. 9 1685-99 PubMed GONUTS page

[PMID:22475386-1] 1.0 ^1.1 Craig, DB et al. (2012) Random mutagenesis suggests that sequence errors are not a major cause of variation in the activity of individual molecules of β-galactosidase. Biochem. Cell Biol. 90 540-7 PubMed GONUTS page

[PMID:21873635-2] 2.0 ^2.1 ^2.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:25953817-3] Bartesaghi, A et al. (2015) 2.2 Å resolution cryo-EM structure of β-galactosidase in complex with a cell-permeant inhibitor. Science 348 1147-51 PubMed GONUTS page

[PMID:24613486-4] Vinothkumar, KR et al. (2014) Molecular mechanism of antibody-mediated activation of β-galactosidase. Structure 22 621-7 PubMed GONUTS page

[PMID:23850452-5] Hall, Z et al. (2013) The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes. Structure 21 1325-37 PubMed GONUTS page

[PMID:4860414-6] Neville, MC & Ling, GN (1967) Synergistic activation of beta-galactosidase by Na and Cs. Arch. Biochem. Biophys. 118 596-610 PubMed GONUTS page

[PMID:11732897-7] Juers, DH et al. (2001) A structural view of the action of Escherichia coli (lacZ) beta-galactosidase. Biochemistry 40 14781-94 PubMed GONUTS page

[PMID:8008071-8] Jacobson, RH et al. (1994) Three-dimensional structure of beta-galactosidase from E. coli. Nature 369 761-6 PubMed GONUTS page

[PMID:14304855-9] 9.0 ^9.1 CRAVEN, GR et al. (1965) PURIFICATION, COMPOSITION, AND MOLECULAR WEIGHT OF THE BETA-GALACTOSIDASE OF ESCHERICHIA COLI K12. J. Biol. Chem. 240 2468-77 PubMed GONUTS page

[PMID:14022758-10] COOK, A & LEDERBERG, J (1962) Recombination studies of lactose nonfermenting mutants of Escherichia coli K-12. Genetics 47 1335-53 PubMed GONUTS page

[PMID:4625429-11] Tenu, JP et al. (1972) Kinetic study of the activation process of -galactosidase from Escherichia coli by Mg 2+ . Eur. J. Biochem. 26 112-8 PubMed GONUTS page

[PMID:11045615-12] Juers, DH et al. (2000) High resolution refinement of beta-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for alpha-complementation. Protein Sci. 9 1685-99 PubMed GONUTS page

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ECOLI:BGAL

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