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UniProtKB - P00722 (BGAL_ECOLI)
Protein
Beta-galactosidase
Gene
lacZ
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalytic activityi
- Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. EC:3.2.1.23
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.
- KM=0.04 mM for p-nitrophenyl beta-D-galactoside6 Publications
- KM=0.12 mM for o-nitrophenyl beta-D-galactoside6 Publications
- KM=0.15 mM for 2,3-dinitrophenyl beta-D-galactopyranoside6 Publications
- KM=0.41 mM for 2,5-dinitrophenyl beta-D-galactopyranoside6 Publications
- KM=11.6 mM for p-nitrophenol-alpha-L-arabinopyranoside6 Publications
- KM=16.9 mM for p-nitrophenol-beta-D-fucopyranoside6 Publications
- KM=34 µM for p-nitrophenyl beta-D-galactoside (with magnesium as cofactor and 30 degrees Celsius)6 Publications
- KM=140 µM for o-nitrophenyl beta-D-galactoside (with magnesium as cofactor and 30 degrees Celsius)6 Publications
- KM=940 µM for allolactose (with magnesium as cofactor and 30 degrees Celsius)6 Publications
- 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 key | Position(s) | DescriptionActions | Graphical view | 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
- beta-galactosidase activity Source: EcoCyc
- carbohydrate binding Source: InterPro
- identical protein binding Source: IntAct
- magnesium ion binding Source: EcoCyc
GO - Biological processi
- lactose catabolic process Source: EcoCyc
Keywordsi
Molecular function | Glycosidase, Hydrolase |
Ligand | Magnesium, Manganese, Metal-binding, Sodium |
Enzyme and pathway databases
BioCyci | EcoCyc:BETAGALACTOSID-MONOMER |
BRENDAi | 3.2.1.23, 2026 |
SABIO-RKi | P00722 |
Protein family/group databases
CAZyi | GH2, Glycoside Hydrolase Family 2 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:lacZ Ordered Locus Names:b0344, JW0335 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | 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 |
Miscellaneous databases
PHI-basei | PHI:6268 |
Chemistry databases
ChEMBLi | CHEMBL4603 |
DrugBanki | DB02294, (5R,6S,7S,8S)-5-hydroxymethyl-6,7,8-trihydroxy-tetrazolo[1,5-A]piperidine DB01920, 1-O-[O-Nitrophenyl]-Beta-D-Galactopyranose DB02228, 2-deoxy-2-fluoro-Beta-D-galactose DB04382, 2-Deoxy-alpha-D-galactopyranose 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 DB04530, S,S-(2-Hydroxyethyl)Thiocysteine DB13503, Tyrothricin |
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 PublicationsBinary interactionsi
P00722
With | #Exp. | IntAct |
---|---|---|
itself | 3 | EBI-369998,EBI-369998 |
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
DIPi | DIP-10081N |
IntActi | P00722, 76 interactors |
STRINGi | 511145.b0344 |
Chemistry databases
BindingDBi | P00722 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
PCDDBi | P00722 |
SMRi | P00722 |
ModBasei | Search... |
PDBe-KBi | 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 | COG3250, Bacteria |
HOGENOMi | CLU_002346_0_2_6 |
InParanoidi | P00722 |
PhylomeDBi | P00722 |
Family and domain databases
Gene3Di | 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 | PTHR46323, PTHR46323, 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 |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P00722-1 [UniParc]FASTAAdd to basket
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
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_SSZK01000061.1 |
Genome annotation databases
EnsemblBacteriai | AAC73447; AAC73447; b0344 BAE76126; BAE76126; BAE76126 |
GeneIDi | 945006 |
KEGGi | ecj:JW0335 eco:b0344 |
Similar proteinsi
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_SSZK01000061.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi 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 | [»] | |
6KUZ | X-ray | 2.83 | A/B/C/D | 1-1024 | [»] | |
6TSH | electron microscopy | 2.30 | A/B/C/D | 10-1024 | [»] | |
6TSK | electron microscopy | 2.30 | A/B/C/D | 10-1024 | [»] | |
6TTE | electron microscopy | 2.20 | A/B/C/D | 10-1024 | [»] | |
6X1Q | electron microscopy | 1.80 | A/B/C/D | 3-1023 | [»] | |
7BRS | X-ray | 2.67 | A/B/C/D | 1-1024 | [»] | |
7BTK | X-ray | 2.70 | A/B/C/D | 1-1024 | [»] | |
PCDDBi | P00722 | |||||
SMRi | P00722 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
DIPi | DIP-10081N |
IntActi | P00722, 76 interactors |
STRINGi | 511145.b0344 |
Chemistry databases
BindingDBi | P00722 |
ChEMBLi | CHEMBL4603 |
DrugBanki | DB02294, (5R,6S,7S,8S)-5-hydroxymethyl-6,7,8-trihydroxy-tetrazolo[1,5-A]piperidine DB01920, 1-O-[O-Nitrophenyl]-Beta-D-Galactopyranose DB02228, 2-deoxy-2-fluoro-Beta-D-galactose DB04382, 2-Deoxy-alpha-D-galactopyranose 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 DB04530, S,S-(2-Hydroxyethyl)Thiocysteine DB13503, Tyrothricin |
Protein family/group databases
CAZyi | GH2, Glycoside Hydrolase Family 2 |
Proteomic databases
PaxDbi | P00722 |
PRIDEi | P00722 |
Protocols and materials databases
ABCDi | P00722, 6 sequenced antibodies |
Genome annotation databases
EnsemblBacteriai | AAC73447; AAC73447; b0344 BAE76126; BAE76126; BAE76126 |
GeneIDi | 945006 |
KEGGi | ecj:JW0335 eco:b0344 |
Organism-specific databases
EchoBASEi | EB0522 |
Phylogenomic databases
eggNOGi | COG3250, Bacteria |
HOGENOMi | CLU_002346_0_2_6 |
InParanoidi | P00722 |
PhylomeDBi | P00722 |
Enzyme and pathway databases
BioCyci | EcoCyc:BETAGALACTOSID-MONOMER |
BRENDAi | 3.2.1.23, 2026 |
SABIO-RKi | P00722 |
Miscellaneous databases
EvolutionaryTracei | P00722 |
PHI-basei | PHI:6268 |
PROi | PR:P00722 |
Family and domain databases
Gene3Di | 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 | PTHR46323, PTHR46323, 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 |
MobiDBi | 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: | February 23, 2022 | |
This is version 210 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, Direct protein sequencing, Reference proteomeDocuments
- Glycosyl hydrolases
Classification of glycosyl hydrolase families and list of entries - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families