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P29853 (BGAL_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. 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

EC=3.2.1.23
Alternative name(s):
Lactase-N
Short name=Lactase
INN=Tilactase
Gene names
Name:lacA
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length1006 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.

Catalytic activity

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

Pharmaceutical use

Capable of effecting hydrolysis of lactose in situ in the gastrointestinal tract of lactase-deficient subjects when given as replacement therapy at mealtime.

Sequence similarities

Belongs to the glycosyl hydrolase 35 family.

Ontologies

Keywords
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termPharmaceutical
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionbeta-galactosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 1006987Beta-galactosidase
PRO_0000012192

Sites

Active site2001Proton donor Potential
Active site2981Nucleophile Potential

Amino acid modifications

Glycosylation1561N-linked (GlcNAc...) Potential
Glycosylation3731N-linked (GlcNAc...) Potential
Glycosylation4021N-linked (GlcNAc...) Potential
Glycosylation4221N-linked (GlcNAc...) Potential
Glycosylation4781N-linked (GlcNAc...) Potential
Glycosylation5221N-linked (GlcNAc...) Potential
Glycosylation6221N-linked (GlcNAc...) Potential
Glycosylation7391N-linked (GlcNAc...) Potential
Glycosylation7601N-linked (GlcNAc...) Potential
Glycosylation7771N-linked (GlcNAc...) Potential
Glycosylation8051N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2061S → C in CAA00105. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P29853 [UniParc].

Last modified February 1, 1994. Version 2.
Checksum: 7157B28A83805488

FASTA1,006109,161
        10         20         30         40         50         60 
MKLSSACAIA LLAAQAAGAS IKHRINGFTL TEHSDPAKRE LLQKYVTWDD KSLFINGERI 

        70         80         90        100        110        120 
MIFSGEFHPF RLPVKELQLD IFQKVKALGF NCVSFYVDWA LVEGKPGEYR ADGIFDLEPF 

       130        140        150        160        170        180 
FDAASEAGIY LLARPGPYIN AESSGGGFPG WLQRVNGTLR SSDKAYLDAT DNYVSHVAAT 

       190        200        210        220        230        240 
IAKYQITNGG PIILYQPENE YTSGCSGVEF PDPVYMQYVE DQARNAGVVI PLINNDASAS 

       250        260        270        280        290        300 
GNNAPGTGKG AVDIYGHDSY PLGFDCANPT VWPSGDLPTN FRTLHLEQSP TTPYAIVEFQ 

       310        320        330        340        350        360 
GGSYDPWGGP GFAACSELLN NEFERVFYKN DFSFQIAIMN LYMIFGGTNW GNLGYPNGYT 

       370        380        390        400        410        420 
SYDYGSAVTE SRNITREKYS ELKLLGNFAK VSPGYLTASP GNLTTSGYAD TTDLTVTPLL 

       430        440        450        460        470        480 
GNSTGSFFVV RHSDYSSEES TSYKLRLPTS AGSVTIPQLG GTLTLNGRDS KIHVTDHNVS 

       490        500        510        520        530        540 
GTNIIYSTAE VFTWKKFADG KVLVLYGGAG EHHELAISTK SNVTVIEGSE SGISSKQTSS 

       550        560        570        580        590        600 
SVVVGWDVST TRRIIQVGDL KILLLDRNSA YNYWVPQLAT DGTSPGFSTP EKVASSIIVK 

       610        620        630        640        650        660 
AGYLVRTAYL KGSGLYLTAD FNATTSVEVI GVPSTAKNLF INGDKTSHTV DKNGIWSATV 

       670        680        690        700        710        720 
DYNAPDISLP SLKDLDWKYV DTLPEIQSSY DDSLWPAADL KQTKNTLRSL TTPTSLYSSD 

       730        740        750        760        770        780 
YGFHTGYLLY RGHFTATGNE STFAIDTQGG SAFGSSVWLN GTYLGSWTGL YANSDYNATY 

       790        800        810        820        830        840 
NLPQLQAGKT YVITVVIDNM GLEENWTVGE DLMKSPRGIS TSCLPDGQAA PISWKLTGNL 

       850        860        870        880        890        900 
GGEDYEDKVR GPLNEGGLYA ERQGFHQPEP PSQNWKSSSP LEGLSEAGIG FYSASFDLDL 

       910        920        930        940        950        960 
PKDGMSHCSS TSVTALRHPR TACRSTSTDI VCEIHKQHRT SDQLPCPRGN PELSRNELVG 

       970        980        990       1000 
GDPVALDSAG GKLESLELSY TTPVLTALGE VESVDQPKYK KRKGAY 

« Hide

References

[1]"Saccharomyces cerevisiae cells secreting an Aspergillus niger beta-galactosidase grow on whey permeate."
Kumar V., Ramakrishnan S., Teeri T.T., Knowles J.K., Hartley B.S.
Biotechnology (N.Y.) 10:82-85(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: VTT D-80144.
[2]"DNA construct and modified yeast."
Hartley B.S., Ramakrishnan S., Kumar V.
Patent number WO9010703, 20-SEP-1990
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PHARMACEUTICAL USE.
Strain: VTT D-80144.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L06037 Genomic DNA. Translation: AAA32696.1.
S37150 mRNA. Translation: AAC60538.1.
A00968 Unassigned DNA. Translation: CAA00105.1.
PIRT31685.

3D structure databases

ProteinModelPortalP29853.
SMRP29853. Positions 41-1006.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP29853.
ChEMBLCHEMBL4753.

Protein family/group databases

CAZyGH35. Glycoside Hydrolase Family 35.
mycoCLAPLAC35A_ASPNG.

Proteomic databases

PRIDEP29853.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG1874.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16612.

Family and domain databases

Gene3D2.102.20.10. 1 hit.
2.60.120.260. 2 hits.
2.60.390.10. 1 hit.
3.20.20.80. 1 hit.
InterProIPR018954. Betagal_dom2.
IPR025972. BetaGal_dom3.
IPR025300. BetaGal_jelly_roll_dom.
IPR008979. Galactose-bd-like.
IPR019801. Glyco_hydro_35_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR001944. Glycoside_Hdrlase_35.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR23421. PTHR23421. 1 hit.
PfamPF10435. BetaGal_dom2. 1 hit.
PF13363. BetaGal_dom3. 1 hit.
PF13364. BetaGal_dom4_5. 1 hit.
PF01301. Glyco_hydro_35. 1 hit.
[Graphical view]
PRINTSPR00742. GLHYDRLASE35.
SMARTSM01029. BetaGal_dom2. 1 hit.
[Graphical view]
SUPFAMSSF117100. SSF117100. 1 hit.
SSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEPS01182. GLYCOSYL_HYDROL_F35. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGAL_ASPNG
AccessionPrimary (citable) accession number: P29853
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 1, 1994
Last modified: April 16, 2014
This is version 86 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries