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

P00723 (BGAL_KLULA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:LAC4
Ordered Locus Names:KLLA0B14883g
OrganismKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]
Taxonomic identifier284590 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces

Protein attributes

Sequence length1025 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Sequence similarities

Belongs to the glycosyl hydrolase 2 family.

Ontologies

Keywords
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentbeta-galactosidase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionbeta-galactosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

carbohydrate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10251025Beta-galactosidase
PRO_0000057663

Sites

Active site4821Proton donor By similarity
Active site5511Nucleophile By similarity

Secondary structure

................................................................................................................................................................................. 1025
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00723 [UniParc].

Last modified July 1, 1993. Version 2.
Checksum: AF3136235DB5A464

FASTA1,025117,619
        10         20         30         40         50         60 
MSCLIPENLR NPKKVHENRL PTRAYYYDQD IFESLNGPWA FALFDAPLDA PDAKNLDWET 

        70         80         90        100        110        120 
AKKWSTISVP SHWELQEDWK YGKPIYTNVQ YPIPIDIPNP PTVNPTGVYA RTFELDSKSI 

       130        140        150        160        170        180 
ESFEHRLRFE GVDNCYELYV NGQYVGFNKG SRNGAEFDIQ KYVSEGENLV VVKVFKWSDS 

       190        200        210        220        230        240 
TYIEDQDQWW LSGIYRDVSL LKLPKKAHIE DVRVTTTFVD SQYQDAELSV KVDVQGSSYD 

       250        260        270        280        290        300 
HINFTLYEPE DGSKVYDASS LLNEENGNTT FSTKEFISFS TKKNEETAFK INVKAPEHWT 

       310        320        330        340        350        360 
AENPTLYKYQ LDLIGSDGSV IQSIKHHVGF RQVELKDGNI TVNGKDILFR GVNRHDHHPR 

       370        380        390        400        410        420 
FGRAVPLDFV VRDLILMKKF NINAVRNSHY PNHPKVYDLF DKLGFWVIDE ADLETHGVQE 

       430        440        450        460        470        480 
PFNRHTNLEA EYPDTKNKLY DVNAHYLSDN PEYEVAYLDR ASQLVLRDVN HPSIIIWSLG 

       490        500        510        520        530        540 
NEACYGRNHK AMYKLIKQLD PTRLVHYEGD LNALSADIFS FMYPTFEIME RWRKNHTDEN 

       550        560        570        580        590        600 
GKFEKPLILC EYGHAMGNGP GSLKEYQELF YKEKFYQGGF IWEWANHGIE FEDVSTADGK 

       610        620        630        640        650        660 
LHKAYAYGGD FKEEVHDGVF IMDGLCNSEH NPTPGLVEYK KVIEPVHIKI AHGSVTITNK 

       670        680        690        700        710        720 
HDFITTDHLL FIDKDTGKTI DVPSLKPEES VTIPSDTTYV VAVLKDDAGV LKAGHEIAWG 

       730        740        750        760        770        780 
QAELPLKVPD FVTETAEKAA KINDGKRYVS VESSGLHFIL DKLLGKIESL KVKGKEISSK 

       790        800        810        820        830        840 
FEGSSITFWR PPTNNDEPRD FKNWKKYNID LMKQNIHGVS VEKGSNGSLA VVTVNSRISP 

       850        860        870        880        890        900 
VVFYYGFETV QKYTIFANKI NLNTSMKLTG EYQPPDFPRV GYEFWLGDSY ESFEWLGRGP 

       910        920        930        940        950        960 
GESYPDKKES QRFGLYDSKD VEEFVYDYPQ ENGNHTDTHF LNIKFEGAGK LSIFQKEKPF 

       970        980        990       1000       1010       1020 
NFKISDEYGV DEAAHACDVK RYGRHYLRLD HAIHGVGSEA CGPAVLDQYR LKAQDFNFEF 


DLAFE 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of the Kluyveromyces lactis beta-galactosidase: comparison with prokaryotic enzymes and secondary structure analysis."
Poch O., L'Hote H., Dallery V., Debeaux F., Fleer R., Sodoyer R.
Gene 118:55-63(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Genome evolution in yeasts."
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. expand/collapse author list , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.
[3]"Analysis of a eukaryotic beta-galactosidase gene: the N-terminal end of the yeast Kluyveromyces lactis protein shows homology to the Escherichia coli lacZ gene product."
Breunig K.D., Dahlems U., Das S., Hollenberg C.P.
Nucleic Acids Res. 12:2327-2341(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-119.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M84410 Genomic DNA. Translation: AAA35265.1.
CR382122 Genomic DNA. Translation: CAH02587.1.
X00430 Genomic DNA. Translation: CAA25128.1.
PIRJC1266.
RefSeqXP_452194.1. XM_452194.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3OB8X-ray2.80A/B/C/D2-1025[»]
3OBAX-ray2.75A/B/C/D2-1025[»]
ProteinModelPortalP00723.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING28985.P00723.

Protein family/group databases

CAZyGH2. Glycoside Hydrolase Family 2.

Proteomic databases

PRIDEP00723.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2897170.
KEGGkla:KLLA0B14883g.

Phylogenomic databases

HOGENOMHOG000252444.
KOK01190.
OMARTIERDK.
OrthoDBEOG7ZWD94.

Enzyme and pathway databases

BRENDA3.2.1.23. 2826.
SABIO-RKP00723.

Family and domain databases

Gene3D2.60.120.260. 1 hit.
2.60.40.320. 3 hits.
2.70.98.10. 1 hit.
3.20.20.80. 1 hit.
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.
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...

Other

EvolutionaryTraceP00723.

Entry information

Entry nameBGAL_KLULA
AccessionPrimary (citable) accession number: P00723
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1993
Last modified: May 14, 2014
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries