UniProtKB - P00722 (BGAL_ECOLI)

BLAST

>sp|P00722|BGAL_ECOLI Beta-galactosidase OS=Escherichia coli (strain K12) OX=83333 GN=lacZ PE=1 SV=2
MTMITDSLAVVLQRRDWENPGVTQLNRLAAHPPFASWRNSEEARTDRPSQQLRSLNGEWR
FAWFPAPEAVPESWLECDLPEADTVVVPSNWQMHGYDAPIYTNVTYPITVNPPFVPTENP
TGCYSLTFNVDESWLQEGQTRIIFDGVNSAFHLWCNGRWVGYGQDSRLPSEFDLSAFLRA
GENRLAVMVLRWSDGSYLEDQDMWRMSGIFRDVSLLHKPTTQISDFHVATRFNDDFSRAV
LEAEVQMCGELRDYLRVTVSLWQGETQVASGTAPFGGEIIDERGGYADRVTLRLNVENPK
LWSAEIPNLYRAVVELHTADGTLIEAEACDVGFREVRIENGLLLLNGKPLLIRGVNRHEH
HPLHGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTLCDRYGLYVVDEANIETHG
MVPMNRLTDDPRWLPAMSERVTRMVQRDRNHPSVIIWSLGNESGHGANHDALYRWIKSVD
PSRPVQYEGGGADTTATDIICPMYARVDEDQPFPAVPKWSIKKWLSLPGETRPLILCEYA
HAMGNSLGGFAKYWQAFRQYPRLQGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDR
QFCMNGLVFADRTPHPALTEAKHQQQFFQFRLSGQTIEVTSEYLFRHSDNELLHWMVALD
GKPLASGEVPLDVAPQGKQLIELPELPQPESAGQLWLTVRVVQPNATAWSEAGHISAWQQ
WRLAENLSVTLPAASHAIPHLTTSEMDFCIELGNKRWQFNRQSGFLSQMWIGDKKQLLTP
LRDQFTRAPLDNDIGVSEATRIDPNAWVERWKAAGHYQAEAALLQCTADTLADAVLITTA
HAWQHQGKTLFISRKTYRIDGSGQMAITVDVEVASDTPHPARIGLNCQLAQVAERVNWLG
LGPQENYPDRLTAACFDRWDLPLSDMYTPYVFPSENGLRCGTRELNYGPHQWRGDFQFNI
SRYSQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSPSVSAEFQLSAGRYHYQLV
WCQK

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History
Entry version 191 (07 Nov 2018)
Sequence version 2 (23 Jan 2007)
Previous versions | rss
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Protein

Beta-galactosidase

Gene

lacZ

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Catalytic activityⁱ

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

Cofactorⁱ

Protein has several cofactor binding sites:

Mg²⁺, Mn²⁺Note: Binds 2 magnesium ions per monomer. Can also use manganese.
Na⁺Note: Binds 1 sodium ion per monomer.

Activity 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.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	103	Substrate	1
Metal bindingⁱ	202	Sodium	1
Binding siteⁱ	202	Substrate	1
Siteⁱ	358	Transition state stabilizer	1
Siteⁱ	392	Transition state stabilizer	1
Metal bindingⁱ	417	Magnesium 11 Publication	1
Metal bindingⁱ	419	Magnesium 11 Publication	1
Active siteⁱ	462	Proton donor1 Publication	1
Metal bindingⁱ	462	Magnesium 11 Publication	1
Binding siteⁱ	462	Substrate	1
Active siteⁱ	538	Nucleophile1 Publication	1
Metal bindingⁱ	598	Magnesium 21 Publication	1
Metal bindingⁱ	602	Sodium; via carbonyl oxygen	1
Metal bindingⁱ	605	Sodium	1
Binding siteⁱ	605	Substrate	1
Binding siteⁱ	1000	Substrate	1
Siteⁱ	1000	Important for ensuring that an appropriate proportion of lactose is converted to allolactose	1

GO - Molecular functionⁱ

alkali metal ion binding
Source: EcoCyc
Inferred from direct assayⁱ
- 11732897
- 4860414
beta-galactosidase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 14304855
carbohydrate binding Source: InterPro
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
magnesium ion binding
Source: EcoCyc
Inferred from direct assayⁱ
- 11045615
- 4625429

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

lactose catabolic process
Source: CACAO
Inferred from mutant phenotypeⁱ
- 22475386

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Glycosidase, Hydrolase
Ligand	Magnesium, Manganese, Metal-binding, Sodium

Enzyme and pathway databases

BioCycⁱ	EcoCyc:BETAGALACTOSID-MONOMER MetaCyc:BETAGALACTOSID-MONOMER
BRENDAⁱ	3.2.1.23 2026
SABIO-RKⁱ	P00722

Protein family/group databases

Carbohydrate-Active enZymes More...CAZyⁱ	GH2 Glycoside Hydrolase Family 2

CAZyⁱ

GH2 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
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG10527 lacZ

EcoGeneⁱ

EG10527 lacZ

Subcellular locationⁱ

GO - Cellular componentⁱ

beta-galactosidase complex
Source: EcoCyc
Inferred from direct assayⁱ
- 14304855
- 8008071

View the complete GO annotation on QuickGO ...

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	202	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. 1 Publication	1
Mutagenesisⁱ	202	D → F: Obliterates all binding and catalysis. 1 Publication	1
Mutagenesisⁱ	358	H → D, F, L or N: Less stable to heat than wild-type. Causes significant destabilizations of the first transition state. 1 Publication	1
Mutagenesisⁱ	392	H → E, F or K: Essentially inactive unless very rapid purification. Causes very large destabilizations of the transition state. 1 Publication	1
Mutagenesisⁱ	462	E → H: Slowly inactivates galactosidase activity by reducing the binding of magnesium. It increases binding specificity. 1 Publication	1
Mutagenesisⁱ	538	E → Q: 10000-fold decrease in the beta-galactosidase activity. 1 Publication	1
Mutagenesisⁱ	541	H → E, F or N: Poorly reactive with galactosyl substrates. Less stable to heat than wild-type. 1 Publication	1
Mutagenesisⁱ	602	F → A: Decreases the stability of the loop 794-804. 1 Publication	1
Mutagenesisⁱ	795	G → A: It forces the apoenzyme to adopt the closed rather than the open conformation. Reduces the binding affinity. 1 Publication	1
Mutagenesisⁱ	798	E → A or L: The catalytic efficiency is not increased, when the sodium concentration increases. 1 Publication	1
Mutagenesisⁱ	798	E → D or Q: Small increase of the catalytic efficiency, when the sodium concentration increases. 1 Publication	1
Mutagenesisⁱ	1000	W → F, G, L or T: Decreases affinity for substrate. 1 Publication	1

Chemistry databases

ChEMBLⁱ	CHEMBL4603
Drug and drug target database More...DrugBankⁱ	DB01920 1-O-[O-Nitrophenyl]-Beta-D-Galactopyranose DB02228 2-deoxy-2-fluoro-Beta-D-galactose DB04382 2-Deoxy-Beta-D-Galactose DB04155 2-Fluoro-2-Deoxy-Beta-D-Galactopyranosyl-Beta-D-Glucopyranose DB02632 4-nitrophenyl-beta-D-galactoside DB04116 Allolactose DB01885 D-Galctopyranosyl-1-On DB01862 Isopropyl beta-D-thiogalactopyranoside DB04465 Lactose

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		Removed1 Publication
ChainⁱPRO_0000057650	2 – 1024	Beta-galactosidaseAdd BLAST		1023

Proteomic databases

PaxDbⁱ	P00722
PRIDEⁱ	P00722

Expressionⁱ

Inductionⁱ

By allolactose.1 Publication

Interactionⁱ

Subunit structureⁱ

Homotetramer.4 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-369998,EBI-369998

With

Entry

#Exp.

IntAct

Notes

itself

EBI-369998,EBI-369998

GO - Molecular functionⁱ

identical protein binding
Source: IntAct
Inferred from physical interactionⁱ

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

Database of interacting proteins More...DIPⁱ	DIP-10081N
IntActⁱ	P00722, 76 interactors
STRINGⁱ	316407.85674486

Chemistry databases

BindingDBⁱ

P00722

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	5 – 7	Combined sources	3
Helixⁱ	11 – 14	Combined sources	4
Helixⁱ	16 – 18	Combined sources	3
Beta strandⁱ	23 – 26	Combined sources	4
Beta strandⁱ	37 – 39	Combined sources	3
Helixⁱ	40 – 45	Combined sources	6
Beta strandⁱ	52 – 54	Combined sources	3
Beta strandⁱ	57 – 66	Combined sources	10
Helixⁱ	67 – 69	Combined sources	3
Helixⁱ	73 – 76	Combined sources	4
Beta strandⁱ	83 – 88	Combined sources	6
Helixⁱ	91 – 94	Combined sources	4
Beta strandⁱ	100 – 105	Combined sources	6
Beta strandⁱ	121 – 130	Combined sources	10
Helixⁱ	132 – 136	Combined sources	5
Beta strandⁱ	137 – 145	Combined sources	9
Beta strandⁱ	147 – 155	Combined sources	9
Beta strandⁱ	158 – 164	Combined sources	7
Beta strandⁱ	166 – 168	Combined sources	3
Beta strandⁱ	170 – 173	Combined sources	4
Turnⁱ	175 – 177	Combined sources	3
Beta strandⁱ	180 – 191	Combined sources	12
Helixⁱ	194 – 198	Combined sources	5
Beta strandⁱ	202 – 205	Combined sources	4
Beta strandⁱ	213 – 218	Combined sources	6
Beta strandⁱ	220 – 232	Combined sources	13
Beta strandⁱ	236 – 249	Combined sources	14
Beta strandⁱ	255 – 263	Combined sources	9
Beta strandⁱ	266 – 275	Combined sources	10
Beta strandⁱ	279 – 281	Combined sources	3
Beta strandⁱ	289 – 298	Combined sources	10
Beta strandⁱ	304 – 307	Combined sources	4
Beta strandⁱ	310 – 318	Combined sources	9
Turnⁱ	319 – 321	Combined sources	3
Beta strandⁱ	323 – 331	Combined sources	9
Beta strandⁱ	336 – 339	Combined sources	4
Beta strandⁱ	342 – 345	Combined sources	4
Beta strandⁱ	352 – 356	Combined sources	5
Turnⁱ	362 – 364	Combined sources	3
Helixⁱ	370 – 382	Combined sources	13
Beta strandⁱ	387 – 389	Combined sources	3
Helixⁱ	397 – 406	Combined sources	10
Beta strandⁱ	409 – 413	Combined sources	5
Beta strandⁱ	421 – 423	Combined sources	3
Turnⁱ	424 – 429	Combined sources	6
Helixⁱ	431 – 433	Combined sources	3
Helixⁱ	434 – 448	Combined sources	15
Beta strandⁱ	454 – 458	Combined sources	5
Beta strandⁱ	461 – 463	Combined sources	3
Helixⁱ	467 – 479	Combined sources	13
Turnⁱ	489 – 491	Combined sources	3
Beta strandⁱ	492 – 494	Combined sources	3
Beta strandⁱ	498 – 500	Combined sources	3
Beta strandⁱ	507 – 509	Combined sources	3
Beta strandⁱ	514 – 516	Combined sources	3
Helixⁱ	521 – 525	Combined sources	5
Beta strandⁱ	534 – 540	Combined sources	7
Beta strandⁱ	543 – 545	Combined sources	3
Helixⁱ	550 – 559	Combined sources	10
Beta strandⁱ	563 – 569	Combined sources	7
Beta strandⁱ	576 – 579	Combined sources	4
Beta strandⁱ	581 – 583	Combined sources	3
Beta strandⁱ	585 – 588	Combined sources	4
Turnⁱ	590 – 593	Combined sources	4
Helixⁱ	600 – 603	Combined sources	4
Helixⁱ	617 – 624	Combined sources	8
Beta strandⁱ	627 – 633	Combined sources	7
Beta strandⁱ	636 – 641	Combined sources	6
Beta strandⁱ	652 – 659	Combined sources	8
Beta strandⁱ	662 – 670	Combined sources	9
Beta strandⁱ	678 – 682	Combined sources	5
Beta strandⁱ	691 – 703	Combined sources	13
Beta strandⁱ	708 – 710	Combined sources	3
Beta strandⁱ	714 – 726	Combined sources	13
Beta strandⁱ	740 – 743	Combined sources	4
Beta strandⁱ	745 – 752	Combined sources	8
Beta strandⁱ	755 – 760	Combined sources	6
Turnⁱ	761 – 763	Combined sources	3
Beta strandⁱ	765 – 771	Combined sources	7
Beta strandⁱ	777 – 784	Combined sources	8
Helixⁱ	791 – 794	Combined sources	4
Beta strandⁱ	799 – 801	Combined sources	3
Beta strandⁱ	804 – 806	Combined sources	3
Helixⁱ	807 – 814	Combined sources	8
Turnⁱ	815 – 818	Combined sources	4
Beta strandⁱ	820 – 830	Combined sources	11
Beta strandⁱ	832 – 845	Combined sources	14
Beta strandⁱ	848 – 860	Combined sources	13
Turnⁱ	861 – 863	Combined sources	3
Beta strandⁱ	865 – 873	Combined sources	9
Beta strandⁱ	875 – 877	Combined sources	3
Beta strandⁱ	881 – 890	Combined sources	10
Beta strandⁱ	894 – 904	Combined sources	11
Beta strandⁱ	915 – 922	Combined sources	8
Helixⁱ	923 – 926	Combined sources	4
Beta strandⁱ	939 – 947	Combined sources	9
Beta strandⁱ	950 – 963	Combined sources	14
Helixⁱ	965 – 970	Combined sources	6
Helixⁱ	974 – 976	Combined sources	3
Beta strandⁱ	981 – 991	Combined sources	11
Beta strandⁱ	999 – 1001	Combined sources	3
Helixⁱ	1006 – 1008	Combined sources	3
Beta strandⁱ	1013 – 1022	Combined sources	10

Show more details

3D structure databases

ProteinModelPortalⁱ	P00722
SMRⁱ	P00722
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P00722

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	538 – 541	Substrate binding		4

Sequence similaritiesⁱ

Belongs to the glycosyl hydrolase 2 family.Curated

Phylogenomic databases

eggNOGⁱ	ENOG4105CNT Bacteria COG3250 LUCA
HOGENOMⁱ	HOG000252443
InParanoidⁱ	P00722
KEGG Orthology (KO) More...KOⁱ	K01190
PhylomeDBⁱ	P00722

Family and domain databases

Gene3Dⁱ	2.60.120.260, 1 hit 2.60.40.10, 2 hits 2.70.98.10, 1 hit
HAMAPⁱ	MF_01687 Beta_gal, 1 hit
InterProⁱ	View protein in InterPro IPR004199 B-gal_small/dom_5 IPR036156 Beta-gal/glucu_dom_sf IPR011013 Gal_mutarotase_sf_dom IPR008979 Galactose-bd-like_sf IPR014718 GH-type_carb-bd IPR006101 Glyco_hydro_2 IPR023232 Glyco_hydro_2_AS IPR023933 Glyco_hydro_2_beta_Galsidase IPR006103 Glyco_hydro_2_cat IPR023230 Glyco_hydro_2_CS IPR006102 Glyco_hydro_2_Ig-like IPR006104 Glyco_hydro_2_N IPR017853 Glycoside_hydrolase_SF IPR013783 Ig-like_fold IPR032312 LacZ_4
PANTHERⁱ	PTHR10066:SF76 PTHR10066:SF76, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02929 Bgal_small_N, 1 hit PF16353 DUF4981, 1 hit PF00703 Glyco_hydro_2, 1 hit PF02836 Glyco_hydro_2_C, 1 hit PF02837 Glyco_hydro_2_N, 1 hit
PRINTSⁱ	PR00132 GLHYDRLASE2
SMARTⁱ	View protein in SMART SM01038 Bgal_small_N, 1 hit
SUPFAMⁱ	SSF49303 SSF49303, 2 hits SSF49785 SSF49785, 1 hit SSF51445 SSF51445, 1 hit SSF74650 SSF74650, 1 hit
PROSITEⁱ	View protein in PROSITE PS00719 GLYCOSYL_HYDROL_F2_1, 1 hit PS00608 GLYCOSYL_HYDROL_F2_2, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P00722-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MTMITDSLAV VLQRRDWENP GVTQLNRLAA HPPFASWRNS EEARTDRPSQ 
        60         70         80         90        100
QLRSLNGEWR FAWFPAPEAV PESWLECDLP EADTVVVPSN WQMHGYDAPI 
       110        120        130        140        150
YTNVTYPITV NPPFVPTENP TGCYSLTFNV DESWLQEGQT RIIFDGVNSA 
       160        170        180        190        200
FHLWCNGRWV GYGQDSRLPS EFDLSAFLRA GENRLAVMVL RWSDGSYLED 
       210        220        230        240        250
QDMWRMSGIF RDVSLLHKPT TQISDFHVAT RFNDDFSRAV LEAEVQMCGE 
       260        270        280        290        300
LRDYLRVTVS LWQGETQVAS GTAPFGGEII DERGGYADRV TLRLNVENPK 
       310        320        330        340        350
LWSAEIPNLY RAVVELHTAD GTLIEAEACD VGFREVRIEN GLLLLNGKPL 
       360        370        380        390        400
LIRGVNRHEH HPLHGQVMDE QTMVQDILLM KQNNFNAVRC SHYPNHPLWY 
       410        420        430        440        450
TLCDRYGLYV VDEANIETHG MVPMNRLTDD PRWLPAMSER VTRMVQRDRN 
       460        470        480        490        500
HPSVIIWSLG NESGHGANHD ALYRWIKSVD PSRPVQYEGG GADTTATDII 
       510        520        530        540        550
CPMYARVDED QPFPAVPKWS IKKWLSLPGE TRPLILCEYA HAMGNSLGGF 
       560        570        580        590        600
AKYWQAFRQY PRLQGGFVWD WVDQSLIKYD ENGNPWSAYG GDFGDTPNDR 
       610        620        630        640        650
QFCMNGLVFA DRTPHPALTE AKHQQQFFQF RLSGQTIEVT SEYLFRHSDN 
       660        670        680        690        700
ELLHWMVALD GKPLASGEVP LDVAPQGKQL IELPELPQPE SAGQLWLTVR 
       710        720        730        740        750
VVQPNATAWS EAGHISAWQQ WRLAENLSVT LPAASHAIPH LTTSEMDFCI 
       760        770        780        790        800
ELGNKRWQFN RQSGFLSQMW IGDKKQLLTP LRDQFTRAPL DNDIGVSEAT 
       810        820        830        840        850
RIDPNAWVER WKAAGHYQAE AALLQCTADT LADAVLITTA HAWQHQGKTL 
       860        870        880        890        900
FISRKTYRID GSGQMAITVD VEVASDTPHP ARIGLNCQLA QVAERVNWLG 
       910        920        930        940        950
LGPQENYPDR LTAACFDRWD LPLSDMYTPY VFPSENGLRC GTRELNYGPH 
       960        970        980        990       1000
QWRGDFQFNI SRYSQQQLME TSHRHLLHAE EGTWLNIDGF HMGIGGDDSW 
      1010       1020 
SPSVSAEFQL SAGRYHYQLV WCQK

Length:1,024

Mass (Da):116,483

Last modified:January 23, 2007 - v2

Checksum:ⁱ9D295EF4CEF90B08

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ 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
NCBI Reference Sequences More...RefSeqⁱ	NP_414878.1, NC_000913.3 WP_000177906.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC73447; AAC73447; b0344 BAE76126; BAE76126; BAE76126
GeneIDⁱ	945006
KEGGⁱ	ecj:JW0335 eco:b0344

Protein	Similar proteins		Species	Score	Length	Source
P00722	Beta-galactosidase		Shigella sp.		1024	UniRef100_P00722
Beta-galactosidase		ECOLI		1024
Beta-galactosidase		Escherichia coli str. K-12 substr. MG1655		1024
Beta-galactosidase		ECOLX		1024
Beta-galactosidase		SHIBO		1024
+11

Protein	Similar proteins		Species	Score	Length	Source
P00722	Beta-galactosidase		ECOLX		1029	UniRef90_P00722
Beta-galactosidase 2		KLEP7		1024
Beta-galactosidase		KLEPN		1024
Beta-galactosidase		ECO24		1024
Beta-galactosidase		ECO27		1024
+2111

Protein	Similar proteins		Species	Score	Length	Source
P00722	Beta-galactosidase		ECOLX		1029	UniRef50_P00722
Beta-galactosidase		SHIDS		1024
Beta-galactosidase		ECO57		1024
Beta-galactosidase		ECOHS		1024
Beta-galactosidase		KLEPN		1024
+4943

Cross-referencesⁱ

Web resourcesⁱ

Worthington enzyme manual

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ 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 WP_000177906.1, NZ_LN832404.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1DP0	X-ray	1.70	A/B/C/D	10-1024	[»]
	1F4A	X-ray	2.80	A/B/C/D	4-1024	[»]
	1F4H	X-ray	2.80	A/B/C/D	4-1024	[»]
	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	[»]
	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	[»]
	3J7H	electron microscopy	3.20	A/B/C/D	1-1024	[»]
	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	[»]
	4TTG	X-ray	1.60	A/B/C/D	15-1024	[»]
	4V40	X-ray	2.50	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P	2-1024	[»]
	4V41	X-ray	2.50	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P	2-1024	[»]
	4V44	X-ray	2.70	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P	2-1024	[»]
	4V45	X-ray	2.60	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P	2-1024	[»]
	5A1A	electron microscopy	2.20	A/B/C/D	3-1024	[»]
	6CVM	electron microscopy	1.90	A/B/C/D	3-1023	[»]
	6DRV	electron microscopy	2.20	A/B/C/D	1-1024	[»]
ProteinModelPortalⁱ	P00722
SMRⁱ	P00722
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

DIPⁱ	DIP-10081N
IntActⁱ	P00722, 76 interactors
STRINGⁱ	316407.85674486

Chemistry databases

BindingDBⁱ	P00722
ChEMBLⁱ	CHEMBL4603
DrugBankⁱ	DB01920 1-O-[O-Nitrophenyl]-Beta-D-Galactopyranose DB02228 2-deoxy-2-fluoro-Beta-D-galactose DB04382 2-Deoxy-Beta-D-Galactose DB04155 2-Fluoro-2-Deoxy-Beta-D-Galactopyranosyl-Beta-D-Glucopyranose DB02632 4-nitrophenyl-beta-D-galactoside DB04116 Allolactose DB01885 D-Galctopyranosyl-1-On DB01862 Isopropyl beta-D-thiogalactopyranoside DB04465 Lactose

Protein family/group databases

CAZyⁱ	GH2 Glycoside Hydrolase Family 2

CAZyⁱ

GH2 Glycoside Hydrolase Family 2

Proteomic databases

PaxDbⁱ	P00722
PRIDEⁱ	P00722

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC73447; AAC73447; b0344 BAE76126; BAE76126; BAE76126
GeneIDⁱ	945006
KEGGⁱ	ecj:JW0335 eco:b0344

Organism-specific databases

EchoBASEⁱ	EB0522
EcoGeneⁱ	EG10527 lacZ

Phylogenomic databases

eggNOGⁱ	ENOG4105CNT Bacteria COG3250 LUCA
HOGENOMⁱ	HOG000252443
InParanoidⁱ	P00722
KOⁱ	K01190
PhylomeDBⁱ	P00722

Enzyme and pathway databases

BioCycⁱ	EcoCyc:BETAGALACTOSID-MONOMER MetaCyc:BETAGALACTOSID-MONOMER
BRENDAⁱ	3.2.1.23 2026
SABIO-RKⁱ	P00722

Miscellaneous databases

EvolutionaryTraceⁱ	P00722
Protein Ontology More...PROⁱ	PR:P00722

Family and domain databases

Gene3Dⁱ	2.60.120.260, 1 hit 2.60.40.10, 2 hits 2.70.98.10, 1 hit
HAMAPⁱ	MF_01687 Beta_gal, 1 hit
InterProⁱ	View protein in InterPro IPR004199 B-gal_small/dom_5 IPR036156 Beta-gal/glucu_dom_sf IPR011013 Gal_mutarotase_sf_dom IPR008979 Galactose-bd-like_sf IPR014718 GH-type_carb-bd IPR006101 Glyco_hydro_2 IPR023232 Glyco_hydro_2_AS IPR023933 Glyco_hydro_2_beta_Galsidase IPR006103 Glyco_hydro_2_cat IPR023230 Glyco_hydro_2_CS IPR006102 Glyco_hydro_2_Ig-like IPR006104 Glyco_hydro_2_N IPR017853 Glycoside_hydrolase_SF IPR013783 Ig-like_fold IPR032312 LacZ_4
PANTHERⁱ	PTHR10066:SF76 PTHR10066:SF76, 1 hit
Pfamⁱ	View protein in Pfam PF02929 Bgal_small_N, 1 hit PF16353 DUF4981, 1 hit PF00703 Glyco_hydro_2, 1 hit PF02836 Glyco_hydro_2_C, 1 hit PF02837 Glyco_hydro_2_N, 1 hit
PRINTSⁱ	PR00132 GLHYDRLASE2
SMARTⁱ	View protein in SMART SM01038 Bgal_small_N, 1 hit
SUPFAMⁱ	SSF49303 SSF49303, 2 hits SSF49785 SSF49785, 1 hit SSF51445 SSF51445, 1 hit SSF74650 SSF74650, 1 hit
PROSITEⁱ	View protein in PROSITE PS00719 GLYCOSYL_HYDROL_F2_1, 1 hit PS00608 GLYCOSYL_HYDROL_F2_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	BGAL_ECOLI
Accessionⁱ	P00722Primary (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:	November 7, 2018
	This is version 191 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Glycosyl hydrolases
Classification of glycosyl hydrolase families and list of entries
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

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UniProtKB - P00722 (BGAL_ECOLI)

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Beta-galactosidase

lacZ

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Sites

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GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Kineticsⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ