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Protein

Beta-galactosidase

Gene

lacZ

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotationNote: Binds 2 magnesium ions per monomer.UniRule annotation
  • Na(+)UniRule annotationNote: Binds 1 sodium ion per monomer.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei103 – 1031SubstrateUniRule annotation
Metal bindingi202 – 2021SodiumUniRule annotation
Binding sitei202 – 2021SubstrateUniRule annotation
Sitei358 – 3581Transition state stabilizerUniRule annotation
Sitei392 – 3921Transition state stabilizerUniRule annotation
Metal bindingi417 – 4171Magnesium 1UniRule annotation
Metal bindingi419 – 4191Magnesium 1UniRule annotation
Active sitei462 – 4621Proton donorUniRule annotation
Metal bindingi462 – 4621Magnesium 1UniRule annotation
Binding sitei462 – 4621SubstrateUniRule annotation
Active sitei538 – 5381NucleophileUniRule annotation
Metal bindingi598 – 5981Magnesium 2UniRule annotation
Metal bindingi602 – 6021Sodium; via carbonyl oxygenUniRule annotation
Metal bindingi605 – 6051SodiumUniRule annotation
Binding sitei605 – 6051SubstrateUniRule annotation
Binding sitei1000 – 10001SubstrateUniRule annotation

GO - Molecular functioni

  1. beta-galactosidase activity Source: UniProtKB-EC
  2. carbohydrate binding Source: InterPro
  3. magnesium ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding, Sodium

Enzyme and pathway databases

BioCyciECOL386585:GJFA-391-MONOMER.
ECOO157:LACZ-MONOMER.

Protein family/group databases

CAZyiGH2. Glycoside Hydrolase Family 2.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-galactosidaseUniRule annotation (EC:3.2.1.23UniRule annotation)
Short name:
Beta-galUniRule annotation
Alternative name(s):
LactaseUniRule annotation
Gene namesi
Name:lacZUniRule annotation
Ordered Locus Names:Z0440, ECs0397
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. beta-galactosidase complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10241024Beta-galactosidasePRO_0000366993Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi155864.Z0440.

Structurei

3D structure databases

ProteinModelPortaliQ8X685.
SMRiQ8X685. Positions 14-1024.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the glycosyl hydrolase 2 family.UniRule annotation

Phylogenomic databases

eggNOGiCOG3250.
HOGENOMiHOG000252443.
KOiK01190.
OMAiTNRHEHH.
OrthoDBiEOG6XWV0T.

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.

Q8X685-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTMITDSLAV VLQRRDWENP GVTQLNRLAA HPPFASWRNS EEARTNRPSQ
60 70 80 90 100
QLRSLNGEWQ FVWFPAPEAV PESWLECDLP DADTVVVPSN WQMHGYDAPI
110 120 130 140 150
YTNVTYPITV NPPFVPTENP TGCYSLTFNV DESWLQEGQT RIIFDGVNSA
160 170 180 190 200
FHLWCNGRWV GYGQDSRLLS EFDLSAFLRA GENRLAVMVL RWSDGSYLED
210 220 230 240 250
QDMWRMSGIF RDVSLLHKPT TQISDFHVAT LFNDDFSRAV LEAEVQMYGE
260 270 280 290 300
LRDELRVTVS LWQGETQVAS GTAPFGGEII DERGGYADRV TLGLNVENPK
310 320 330 340 350
LWSAEIPNIY 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 GADTSATDII
510 520 530 540 550
CPMYARVDED QPFPAVPKWS IKKWLSLPGE MRPLILCEYA HAMGNSLGGF
560 570 580 590 600
AKYWQAFRQY PRLQGGFVWD LVDQSLIKYD ENGNPWSAYG GDFGDTPNDR
610 620 630 640 650
QFCMNGLVFA DRTPHPALTE AKHQQQFFQF RLSGRTIEVT SEYLFRHSDN
660 670 680 690 700
ELLHWTVALD GKPLASGEVP LDVAPQGKQV IELPELPRLE STGQLWLTVH
710 720 730 740 750
VVQPNATAWS EAGHISAWQQ WRLAENLSVT LPSAPHAIPQ LTTSETDFCI
760 770 780 790 800
ELDNKRWQFN RQSGFLSQMW IGDKKQLLTP LRDQFTRAPL DNDIGVSEAT
810 820 830 840 850
RIDPNAWVER WKAAGHYQAE AALLQCTADT LADAVLITTV HAWQHQGKTL
860 870 880 890 900
FISRKTYRID GSGQMAITVD VEVASDTPHP ARIGLTCQLA 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):116,410
Last modified:March 1, 2002 - v1
Checksum:iB08BF1EBE7894FE3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG54693.1.
BA000007 Genomic DNA. Translation: BAB33820.1.
PIRiA85529.
E90678.
RefSeqiNP_286085.1. NC_002655.2.
NP_308424.1. NC_002695.1.

Genome annotation databases

EnsemblBacteriaiAAG54693; AAG54693; Z0440.
BAB33820; BAB33820; BAB33820.
GeneIDi914499.
957271.
KEGGiece:Z0440.
ecs:ECs0397.
PATRICi18349741. VBIEscCol44059_0391.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG54693.1.
BA000007 Genomic DNA. Translation: BAB33820.1.
PIRiA85529.
E90678.
RefSeqiNP_286085.1. NC_002655.2.
NP_308424.1. NC_002695.1.

3D structure databases

ProteinModelPortaliQ8X685.
SMRiQ8X685. Positions 14-1024.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi155864.Z0440.

Protein family/group databases

CAZyiGH2. Glycoside Hydrolase Family 2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG54693; AAG54693; Z0440.
BAB33820; BAB33820; BAB33820.
GeneIDi914499.
957271.
KEGGiece:Z0440.
ecs:ECs0397.
PATRICi18349741. VBIEscCol44059_0391.

Phylogenomic databases

eggNOGiCOG3250.
HOGENOMiHOG000252443.
KOiK01190.
OMAiTNRHEHH.
OrthoDBiEOG6XWV0T.

Enzyme and pathway databases

BioCyciECOL386585:GJFA-391-MONOMER.
ECOO157:LACZ-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
    Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
    , Kuhara S., Shiba T., Hattori M., Shinagawa H.
    DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Entry informationi

Entry nameiBGAL_ECO57
AccessioniPrimary (citable) accession number: Q8X685
Secondary accession number(s): Q7AH58
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 1, 2002
Last modified: January 7, 2015
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.