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Q8X685 (BGAL_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-galactosidase

Short name=Beta-gal
EC=3.2.1.23
Alternative name(s):
Lactase
Gene names
Name:lacZ
Ordered Locus Names:Z0440, ECs0397
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length1024 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP-Rule MF_01687

Binds 1 sodium ion per monomer By similarity. HAMAP-Rule MF_01687

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_01687

Sequence similarities

Belongs to the glycosyl hydrolase 2 family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10241024Beta-galactosidase HAMAP-Rule MF_01687
PRO_0000366993

Regions

Region538 – 5414Substrate binding By similarity

Sites

Active site4621Proton donor By similarity
Active site5381Nucleophile By similarity
Metal binding2021Sodium By similarity
Metal binding4171Magnesium 1 By similarity
Metal binding4191Magnesium 1 By similarity
Metal binding4621Magnesium 1 By similarity
Metal binding5981Magnesium 2 By similarity
Metal binding6021Sodium; via carbonyl oxygen By similarity
Metal binding6051Sodium By similarity
Binding site1031Substrate By similarity
Binding site2021Substrate By similarity
Binding site4621Substrate By similarity
Binding site6051Substrate By similarity
Binding site10001Substrate By similarity
Site3581Transition state stabilizer By similarity
Site3921Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8X685 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: B08BF1EBE7894FE3

FASTA1,024116,410
        10         20         30         40         50         60 
MTMITDSLAV VLQRRDWENP GVTQLNRLAA HPPFASWRNS EEARTNRPSQ QLRSLNGEWQ 

        70         80         90        100        110        120 
FVWFPAPEAV PESWLECDLP DADTVVVPSN WQMHGYDAPI YTNVTYPITV NPPFVPTENP 

       130        140        150        160        170        180 
TGCYSLTFNV DESWLQEGQT RIIFDGVNSA FHLWCNGRWV GYGQDSRLLS EFDLSAFLRA 

       190        200        210        220        230        240 
GENRLAVMVL RWSDGSYLED QDMWRMSGIF RDVSLLHKPT TQISDFHVAT LFNDDFSRAV 

       250        260        270        280        290        300 
LEAEVQMYGE LRDELRVTVS LWQGETQVAS GTAPFGGEII DERGGYADRV TLGLNVENPK 

       310        320        330        340        350        360 
LWSAEIPNIY 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 GADTSATDII CPMYARVDED QPFPAVPKWS IKKWLSLPGE MRPLILCEYA 

       550        560        570        580        590        600 
HAMGNSLGGF AKYWQAFRQY PRLQGGFVWD LVDQSLIKYD ENGNPWSAYG GDFGDTPNDR 

       610        620        630        640        650        660 
QFCMNGLVFA DRTPHPALTE AKHQQQFFQF RLSGRTIEVT SEYLFRHSDN ELLHWTVALD 

       670        680        690        700        710        720 
GKPLASGEVP LDVAPQGKQV IELPELPRLE STGQLWLTVH VVQPNATAWS EAGHISAWQQ 

       730        740        750        760        770        780 
WRLAENLSVT LPSAPHAIPQ LTTSETDFCI ELDNKRWQFN RQSGFLSQMW IGDKKQLLTP 

       790        800        810        820        830        840 
LRDQFTRAPL DNDIGVSEAT RIDPNAWVER WKAAGHYQAE AALLQCTADT LADAVLITTV 

       850        860        870        880        890        900 
HAWQHQGKTL FISRKTYRID GSGQMAITVD VEVASDTPHP ARIGLTCQLA 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 

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References

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG54693.1.
BA000007 Genomic DNA. Translation: BAB33820.1.
PIRA85529.
E90678.
RefSeqNP_286085.1. NC_002655.2.
NP_308424.1. NC_002695.1.

3D structure databases

ProteinModelPortalQ8X685.
SMRQ8X685. Positions 14-1024.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z0440.

Protein family/group databases

CAZyGH2. Glycoside Hydrolase Family 2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG54693; AAG54693; Z0440.
BAB33820; BAB33820; BAB33820.
GeneID914499.
957271.
KEGGece:Z0440.
ecs:ECs0397.
PATRIC18349741. VBIEscCol44059_0391.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3250.
HOGENOMHOG000252443.
KOK01190.
OMANPPFVPK.
OrthoDBEOG6XWV0T.

Enzyme and pathway databases

BioCycECOL386585:GJFA-391-MONOMER.
ECOO157:LACZ-MONOMER.

Family and domain databases

Gene3D2.60.120.260. 1 hit.
2.60.40.320. 2 hits.
2.70.98.10. 1 hit.
3.20.20.80. 1 hit.
HAMAPMF_01687. Beta_gal.
InterProIPR004199. 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]
PfamPF02929. 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]
PRINTSPR00132. GLHYDRLASE2.
SMARTSM01038. Bgal_small_N. 1 hit.
[Graphical view]
SUPFAMSSF49303. SSF49303. 2 hits.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF74650. SSF74650. 1 hit.
PROSITEPS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGAL_ECO57
AccessionPrimary (citable) accession number: Q8X685
Secondary accession number(s): Q7AH58
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 1, 2002
Last modified: May 14, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries