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C3NVQ6 (C3NVQ6_VIBCJ) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 33. Feed History...

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

Names and origin

Protein namesRecommended name:
Beta-galactosidase HAMAP-Rule MF_01687
Short name=Beta-gal HAMAP-Rule MF_01687
EC=3.2.1.23 HAMAP-Rule MF_01687
Alternative name(s):
Lactase HAMAP-Rule MF_01687
Gene names
Name:lacZ HAMAP-Rule MF_01687
Ordered Locus Names:VCD_002010
OrganismVibrio cholerae serotype O1 (strain MJ-1236) [Complete proteome] [HAMAP] EMBL ACQ60179.1
Taxonomic identifier593588 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio ›

Protein attributes

Sequence length1044 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. SAAS SAAS013812 HAMAP-Rule MF_01687

Cofactor

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

Binds 2 magnesium ions 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. HAMAP-Rule MF_01687

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region555 – 5584Substrate binding By similarity HAMAP-Rule MF_01687

Sites

Active site4791Proton donor By similarity HAMAP-Rule MF_01687
Active site5551Nucleophile By similarity HAMAP-Rule MF_01687
Metal binding2181Sodium By similarity HAMAP-Rule MF_01687
Metal binding4341Magnesium 1 By similarity HAMAP-Rule MF_01687
Metal binding4361Magnesium 1 By similarity HAMAP-Rule MF_01687
Metal binding4791Magnesium 1 By similarity HAMAP-Rule MF_01687
Metal binding6151Magnesium 2 By similarity HAMAP-Rule MF_01687
Metal binding6191Sodium; via carbonyl oxygen By similarity HAMAP-Rule MF_01687
Metal binding6221Sodium By similarity HAMAP-Rule MF_01687
Binding site1201Substrate By similarity HAMAP-Rule MF_01687
Binding site2181Substrate By similarity HAMAP-Rule MF_01687
Binding site4791Substrate By similarity HAMAP-Rule MF_01687
Binding site6221Substrate By similarity HAMAP-Rule MF_01687
Binding site10151Substrate By similarity HAMAP-Rule MF_01687
Site3751Transition state stabilizer By similarity HAMAP-Rule MF_01687
Site4091Transition state stabilizer By similarity HAMAP-Rule MF_01687

Sequences

Sequence LengthMass (Da)Tools
C3NVQ6 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: 2AF5D57EC04B6908

FASTA1,044120,685
        10         20         30         40         50         60 
MYAVEQRRYW LVASRIQEDL MRNFSDILLS QDWQNPHIVK WHCRTPHVPL HSYRTEQEAR 

        70         80         90        100        110        120 
LDVGGNRQSL NGQWRFALFE KPEAVEPAVI DPDFDDSAWA HIPVPSNWQM QGFDKPIYTN 

       130        140        150        160        170        180 
IQYPFADRPP YVPQDNPTGC YRHRFTLEKQ ALTESIRIVF DGVNSAFHLW CNGHWVGYSQ 

       190        200        210        220        230        240 
DSRLPAEFEL TPYLQEGENL LVAMVLRWSD GSYLEDQDMW WLSGIFRDVY LYRKPILAIE 

       250        260        270        280        290        300 
DFFIRTELDA LYQHAELRVE TRLSQVTRHH QVQVALFDAQ GECVARSQAL HTGQRVVDEK 

       310        320        330        340        350        360 
GAWHDKTEHS LAICSPTLWS DEAPYLYRCV ICLLDEDGAP IEFESAAVGF RKVEITQGLL 

       370        380        390        400        410        420 
KLNGQPLLIR GVNRHEHHPE LGHVMDEASM RRDIELMKQH NFNAVRTAHY PNHPRWYELC 

       430        440        450        460        470        480 
DEYGLYVVDE ANLETHGQFP MSRLSNDPQW VNAYLQRMIG MVERDKNHPC VIIWSLGNES 

       490        500        510        520        530        540 
GIGTNHHAMY QWTKQRDPSR PVQYEGGGAN TAATDIVCPM YARVDQHQPH PAVPKYALKN 

       550        560        570        580        590        600 
WISLPQENRP LILCEYAHAM GNSLGAFYKY WQAFREFPRL QGGFIWDWVD QGISKWDSEG 

       610        620        630        640        650        660 
RHYWGYGGDF GDTINDRQFC INGLLFPDRT PHPALHEVKK VQQPYQFSLS YPKLTIHNER 

       670        680        690        700        710        720 
LFAALPLELV VSVLCDGQEI KQERLPLDIA PRGTITLDLA SLPMLPEHEY HLNAVLLCRE 

       730        740        750        760        770        780 
DQPWSNAGHC IASEQWCLQP RRSMLPKITH APLPQWQQDG DKVRIEAANQ QWQFNRQTGL 

       790        800        810        820        830        840 
LEQWWQNGQP VLSEPLRDNF YRAVLDNDIG TSEAQHLDPN SWIARWHAAG LDKLRVECDD 

       850        860        870        880        890        900 
LRVTTLNESV EVVIDVAHYH QQALALRTRW RYQIFGDARV ELNVEVMLCS DLPPLPRVGL 

       910        920        930        940        950        960 
TLALPVAENP VSWFGRGPHE NYPDRLQSAH VGRYTATVDE LHTPYIFPSE NGLRCDTRQL 

       970        980        990       1000       1010       1020 
QVGALVVEGH FHFSLSRYSQ TMLDKAKHSN ELVAGDKWYL NLDAQHMGVG GDDSWSQSVH 

      1030       1040 
PEFLLTQPHY QYQLTLRVKA SSPQ

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References

[1]"Comparative genomics reveals mechanism for short-term and long-term clonal transitions in pandemic Vibrio cholerae."
Chun J., Grim C.J., Hasan N.A., Lee J.H., Choi S.Y., Haley B.J., Taviani E., Jeon Y.-S., Kim D.W., Lee J.-H., Brettin T.S., Bruce D.C., Challacombe J.F., Detter J.C., Han C.S., Munk A.C., Chertkov O., Meincke L. expand/collapse author list , Saunders E., Walters R.A., Huq A., Nair G.B., Colwell R.R.
Proc. Natl. Acad. Sci. U.S.A. 106:15442-15447(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MJ-1236.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001485 Genomic DNA. Translation: ACQ60179.1.
RefSeqYP_002877749.1. NC_012668.1.

3D structure databases

ProteinModelPortalC3NVQ6.
ModBaseSearch...

Protein-protein interaction databases

STRING593588.VCD_002010.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACQ60179; ACQ60179; VCD_002010.
GeneID7855259.
KEGGvcj:VCD_002010.
PATRIC20075382. VBIVibCho20143_2033.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3250.
HOGENOMHOG000252443.
KOK01190.
OMATIREYHI.
ProtClustDBPRK09525.

Family and domain databases

Gene3D2.60.40.320. 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]
SUPFAMSSF49785. Gal_bind_like. 1 hit.
SSF74650. Gal_mut_like. 1 hit.
SSF49303. Glyco_hydro_2Ig. 2 hits.
SSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC3NVQ6_VIBCJ
AccessionPrimary (citable) accession number: C3NVQ6
Entry history
Integrated into UniProtKB/TrEMBL: June 16, 2009
Last sequence update: June 16, 2009
Last modified: May 1, 2013
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info