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C5A125 (C5A125_ECOBW) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 39. 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:BWG_3744
OrganismEscherichia coli (strain K12 / MC4100 / BW2952) [Complete proteome] [HAMAP]
Taxonomic identifier595496 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length1080 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate By similarity. RuleBase RU000601

Catalytic activity

Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. HAMAP-Rule MF_01687 SAAS SAAS013812

L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H2O. RuleBase RU000601 SAAS SAAS002028

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

Pathway

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. RuleBase RU000601

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_01687

Tetramer of two alpha and two beta chains By similarity. RuleBase RU000601

Sequence similarities

Belongs to the TrpA family. RuleBase RU003662

Belongs to the glycosyl hydrolase 2 family. HAMAP-Rule MF_01687

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region594 – 5974Substrate binding By similarity HAMAP-Rule MF_01687

Sites

Active site5181Proton donor By similarity HAMAP-Rule MF_01687
Active site5941Nucleophile By similarity HAMAP-Rule MF_01687
Metal binding2581Sodium By similarity HAMAP-Rule MF_01687
Metal binding4731Magnesium 1 By similarity HAMAP-Rule MF_01687
Metal binding4751Magnesium 1 By similarity HAMAP-Rule MF_01687
Metal binding5181Magnesium 1 By similarity HAMAP-Rule MF_01687
Metal binding6541Magnesium 2 By similarity HAMAP-Rule MF_01687
Metal binding6581Sodium; via carbonyl oxygen By similarity HAMAP-Rule MF_01687
Metal binding6611Sodium By similarity HAMAP-Rule MF_01687
Binding site1591Substrate By similarity HAMAP-Rule MF_01687
Binding site2581Substrate By similarity HAMAP-Rule MF_01687
Binding site5181Substrate By similarity HAMAP-Rule MF_01687
Binding site6611Substrate By similarity HAMAP-Rule MF_01687
Binding site10561Substrate By similarity HAMAP-Rule MF_01687
Site4141Transition state stabilizer By similarity HAMAP-Rule MF_01687
Site4481Transition state stabilizer By similarity HAMAP-Rule MF_01687

Sequences

Sequence LengthMass (Da)Tools
C5A125 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: D1F2C0191BA208FB

FASTA1,080122,553
        10         20         30         40         50         60 
MERYESLFAQ LKERKEGAFV PFVTLGDPGI EQSLKIIDTL IEAGADALEL GIPFSDPLAI 

        70         80         90        100        110        120 
TDSLAVVLQR RDWENPGVTQ LNRLAAHPPF ASWRNSEEAR TDRPSQQLRS LNGEWRFAWF 

       130        140        150        160        170        180 
PAPEAVPESW LECDLPEADT VVVPSNWQMH GYDAPIYTNV TYPITVNPPF VPTENPTGCY 

       190        200        210        220        230        240 
SLTFNVDESW LQEGQTRIIF DGVNSAFHLW CNGRWVGYGQ DSRLPSEFDL SAFLRAGENR 

       250        260        270        280        290        300 
LAVMVLRWSD GSYLEDQDMW RMSGIFRDVS LLHKPTTQIS DFHVATRFND DFSRAVLEAE 

       310        320        330        340        350        360 
VQMCGELRDY LRVTVSLWQG ETQVASGTAP FGGEIIDERG GYADRVTLRL NVENPKLWSA 

       370        380        390        400        410        420 
EIPNLYRAVV ELHTADGTLI EAEACDVGFR EVRIENGLLL LNGKPLLIRG VNRHEHHPLH 

       430        440        450        460        470        480 
GQVMDEQTMV QDILLMKQNN FNAVRCSHYP NHPLWYTLCD RYGLYVVDEA NIETHGMVPM 

       490        500        510        520        530        540 
NRLTDDPRWL PAMSERVTRM VQRDRNHPSV IIWSLGNESG HGANHDALYR WIKSVDPSRP 

       550        560        570        580        590        600 
VQYEGGGADT TATDIICPMY ARVDEDQPFP AVPKWSIKKW LSLPGETRPL ILCEYAHAMG 

       610        620        630        640        650        660 
NSLGGFAKYW QAFRQYPRLQ GGFVWDWVDQ SLIKYDENGN PWSAYGGDFG DTPNDRQFCM 

       670        680        690        700        710        720 
NGLVFADRTP HPALTEAKHQ QQFFQFRLSG QTIEVTSEYL FRHSDNELLH WMVALDGKPL 

       730        740        750        760        770        780 
ASGEVPLDVA PQGKQLIELP ELPQPESAGQ LWLTVRVVQP NATAWSEAGH ISAWQQWRLA 

       790        800        810        820        830        840 
ENLSVTLPAA SHAIPHLTTS EMDFCIELGN KRWQFNRQSG FLSQMWIGDK KQLLTPLRDQ 

       850        860        870        880        890        900 
FTRAPLDNDI GVSEATRIDP NAWVERWKAA GHYQAEAALL QCTADTLADA VLITTAHAWQ 

       910        920        930        940        950        960 
HQGKTLFISR KTYRIDGSGQ MAITVDVEVA SDTPHPARIG LNCQLAQVAE RVNWLGLGPQ 

       970        980        990       1000       1010       1020 
ENYPDRLTAA CFDRWDLPLS DMYTPYVFPS ENGLRCGTRE LNYGPHQWRG DFQFNISRYS 

      1030       1040       1050       1060       1070       1080 
QQQLMETSHR HLLHAEEGTW LNIDGFHMGI GGDDSWSPSV SAEFQLSAGR YHYQLVWCQK

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References

[1]"Genomic sequencing reveals regulatory mutations and recombinational events in the widely used MC4100 lineage of Escherichia coli K-12."
Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R., Wang L.
J. Bacteriol. 191:4025-4029(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MC4100 / BW2952.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001396 Genomic DNA. Translation: ACR62057.1.
RefSeqYP_002928937.1. NC_012759.1.

3D structure databases

ProteinModelPortalC5A125.
ModBaseSearch...

Protein-protein interaction databases

STRING595496.BWG_3744.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACR62057; ACR62057; BWG_3744.
GeneID7954107.
KEGGebw:BWG_3744.
PATRIC18277261. VBIEscCol60876_4092.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3250.
HOGENOMHOG000252443.
KOK01190.
OMADFHVATH.
ProtClustDBPRK09525.

Enzyme and pathway databases

BioCycECOL595496:GI18-515-MONOMER.
UniPathwayUPA00035; UER00044.

Family and domain databases

Gene3D2.60.40.320. 2 hits.
2.70.98.10. 1 hit.
3.20.20.70. 1 hit.
3.20.20.80. 1 hit.
HAMAPMF_01687. Beta_gal.
InterProIPR013785. Aldolase_TIM.
IPR004199. 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.
IPR011060. RibuloseP-bd_barrel.
IPR002028. Trp_synthase_suA.
[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.
PF00290. Trp_syntA. 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.
SSF51366. RibP_bind_barrel. 1 hit.
PROSITEPS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC5A125_ECOBW
AccessionPrimary (citable) accession number: C5A125
Entry history
Integrated into UniProtKB/TrEMBL: July 28, 2009
Last sequence update: July 28, 2009
Last modified: May 1, 2013
This is version 39 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