Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A5F5U6 (BGAL_VIBC3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. 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:VC0395_A1917, VC395_2453
OrganismVibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395) [Complete proteome] [HAMAP]
Taxonomic identifier345073 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

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.

Sequence caution

The sequence ABQ20296.1 differs from that shown. Reason: Erroneous initiation.

The sequence ACP10443.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10241024Beta-galactosidase HAMAP-Rule MF_01687
PRO_0000367011

Regions

Region535 – 5384Substrate binding By similarity

Sites

Active site4591Proton donor By similarity
Active site5351Nucleophile By similarity
Metal binding1981Sodium By similarity
Metal binding4141Magnesium 1 By similarity
Metal binding4161Magnesium 1 By similarity
Metal binding4591Magnesium 1 By similarity
Metal binding5951Magnesium 2 By similarity
Metal binding5991Sodium; via carbonyl oxygen By similarity
Metal binding6021Sodium By similarity
Binding site1001Substrate By similarity
Binding site1981Substrate By similarity
Binding site4591Substrate By similarity
Binding site6021Substrate By similarity
Binding site9951Substrate By similarity
Site3551Transition state stabilizer By similarity
Site3891Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
A5F5U6 [UniParc].

Last modified March 24, 2009. Version 2.
Checksum: 204F11E6188E33D8

FASTA1,024118,176
        10         20         30         40         50         60 
MRNFSDILLS QDWQNPHIVK WHCRTPHVPL HSYRTEQEAR LDVGGNRQSL NGQWRFALFE 

        70         80         90        100        110        120 
KPEAVEPAVI DPDFDDSAWA HIPVPSNWQM QGFDKPIYTN IQYPFADRPP YVPQDNPTGC 

       130        140        150        160        170        180 
YRHRFTLEKQ ALTESIRIVF DGVNSAFHLW CNGHWVGYSQ DSRLPAEFEL TPYLQEGENL 

       190        200        210        220        230        240 
LVAMVLRWSD GSYLEDQDMW WLSGIFRDVY LYRKPILAIE DFFIRTELDA LYQHAELRVE 

       250        260        270        280        290        300 
TRLSQVTRHH QVQVALFDAQ GECVARSQAL HTGQRVVDEK GAWHDKTEHS LAICSPTLWS 

       310        320        330        340        350        360 
DEAPYLYRCV ICLLDEDGAP IEFESAAVGF RKVEITQGLL KLNGQPLLIR GVNRHEHHPE 

       370        380        390        400        410        420 
LGHVMDEASM RRDIELMKQH NFNAVRTAHY PNHPRWYELC DEYGLYVVDE ANLETHGQFP 

       430        440        450        460        470        480 
MSRLSNDPQW VNAYLQRMIG MVERDKNHPC VIIWSLGNES GIGTNHHAMY QWTKQRDPSR 

       490        500        510        520        530        540 
PVQYEGGGAN TAATDIVCPM YARVDQHQPH PAVPKYALKN WISLPQENRP LILCEYAHAM 

       550        560        570        580        590        600 
GNSLGAFYKY WQAFREFPRL QGGFIWDWVD QGISKWDSEG RHYWGYGGDF GDTINDRQFC 

       610        620        630        640        650        660 
INGLLFPDRT PHPALHEVKK VQQPYQFSLS YPKLTIHNER LFAALPLELV VSVLCDGQEI 

       670        680        690        700        710        720 
KQERLPLDIA PRGTITLDLA SLPMLPEHEY HLNAVLLCRE DQPWSNAGHC IASEQWCLQP 

       730        740        750        760        770        780 
RRSMLPKITH APLPQWQQDG DKVRIEAANQ QWQFNRQTGL LEQWWQNGQP VLSEPLRDNF 

       790        800        810        820        830        840 
YRAVLDNDIG TSEAQHLDPN SWIARWHAAG LDKLRVECDD LRVTTLNESV EVVIDVAHYH 

       850        860        870        880        890        900 
QQALALRTRW RYQIFGDARV ELNVEVMLCS DLPPLPRVGL TLALPVAENP VSWFGRGPHE 

       910        920        930        940        950        960 
NYPDRLQSAH VGRYTATVDE LHTPYIFPSE NGLRCDTRQL QVGALVVEGH FHFSLSRYSQ 

       970        980        990       1000       1010       1020 
TMLDKAKHSN ELVAGDKWYL NLDAQHMGVG GDDSWSQSVH PEFLLTQPHY QYQLTLRVKA 


SSPQ 

« Hide

References

[1]Heidelberg J.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39541 / Classical Ogawa 395 / O395.
[2]"A recalibrated molecular clock and independent origins for the cholera pandemic clones."
Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.
PLoS ONE 3:E4053-E4053(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39541 / Classical Ogawa 395 / O395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000627 Genomic DNA. Translation: ABQ20296.1. Different initiation.
CP001235 Genomic DNA. Translation: ACP10443.1. Different initiation.
RefSeqYP_001217841.1. NC_009457.1.
YP_002820679.1. NC_012582.1.

3D structure databases

ProteinModelPortalA5F5U6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING345073.VC0395_A1917.

Protein family/group databases

CAZyGH2. Glycoside Hydrolase Family 2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ20296; ABQ20296; VC0395_A1917.
ACP10443; ACP10443; VC395_2453.
GeneID5135797.
7776226.
KEGGvco:VC0395_A1917.
vcr:VC395_2453.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3250.
HOGENOMHOG000252443.
KOK01190.

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_VIBC3
AccessionPrimary (citable) accession number: A5F5U6
Secondary accession number(s): C3M461
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 47 of the entry and version 2 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