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

Q700S9 (BGALA_PENSQ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 53. 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:
Probable beta-galactosidase A

EC=3.2.1.23
Alternative name(s):
Lactase A
Gene names
Name:lacA
OrganismPenicillium sp.
Taxonomic identifier5081 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

Protein attributes

Sequence length1011 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 By similarity.

Catalytic activity

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

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 35 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processpolysaccharide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 1011992Probable beta-galactosidase A
PRO_5000072460

Sites

Active site2001Proton donor Potential
Active site2991Nucleophile Potential
Binding site961Substrate
Binding site1401Substrate
Binding site1411Substrate; via amide nitrogen
Binding site1421Substrate
Binding site1991Substrate
Binding site2611Substrate
Binding site3651Substrate

Amino acid modifications

Glycosylation3741N-linked (GlcNAc...) Ref.1
Glycosylation4561N-linked (GlcNAc...) Ref.1
Glycosylation6251N-linked (GlcNAc...) Ref.1
Glycosylation7071N-linked (GlcNAc...) Ref.1
Glycosylation7631N-linked (GlcNAc...) Ref.1
Glycosylation7801N-linked (GlcNAc...) Ref.1
Glycosylation9171N-linked (GlcNAc...) Ref.1
Disulfide bond205 ↔ 206 Ref.1
Disulfide bond267 ↔ 316 Ref.1

Secondary structure

......................................................................................................................................................................... 1011
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q700S9 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: A8A5BD48354F791A

FASTA1,011109,750
        10         20         30         40         50         60 
MKLLSSWVVA ALAAQAAGAA ISHKLDGFTI REHADPAKRA LLQKYVTWDE HSIFVNGERL 

        70         80         90        100        110        120 
MIFSGEVHPY RLPVASLYID IFEKVKALGF NCVSFYVDWA LLEGNPGHYS AEGIFDLQPF 

       130        140        150        160        170        180 
FDAAKEAGIY LLARPGPYIN AEVSGGGFPG WLQRVDGILR TSDEAYLKAT DNYASNIAAT 

       190        200        210        220        230        240 
IAKAQITNGG PIILYQPENE YSGACCGYNG FPDGSYMQYI EDHARDAGIV VPFISNDAWA 

       250        260        270        280        290        300 
AGHNAPGTGA GAVDIYGHDS YPLGFDCANP STWPSGNLPT YFHTSHEQQS PSTPYSLVEF 

       310        320        330        340        350        360 
QGGAFDPWGG VGFAKCAALL NHEFERVFYK NDFSFGVAFL NLYMIFGGTN WGNLGHPGGY 

       370        380        390        400        410        420 
TSYDYGSAIS ESRNITREKY SELKLLGNFA KVSPGYLVAN PGDLSTSTYT NTADLTVTPL 

       430        440        450        460        470        480 
LGSNSSASSF FVIRHSDYSS QASVEYKLTV PTSAGNLTIP QLGGSLTLSG RDSKIHVTDY 

       490        500        510        520        530        540 
DVAGTNILYS TAEVFTWKKF NNEKVLVLYG GPGEHHEFAV SGASSSSVVE GSSSGISSKK 

       550        560        570        580        590        600 
VGKALVVAWD VSTARRIVQV GSLKVFLLDR NSAYNYWVPQ VPTKGTAPGY SNQETTASSI 

       610        620        630        640        650        660 
IVKAGYLVRS AYLDGNDLHI QADFNATTPI EVVGAPSGAK NLVINGKKTQ TKVDKNGIWS 

       670        680        690        700        710        720 
ASVAYTAPKV QLPSLKSLKW KSVDTLPEAK NTYDDSAWTS ADHAYTNNSA HSLQTPTSLF 

       730        740        750        760        770        780 
ASDYGYHTGA LLFRGHFTAN GKEKTFFVQT KGGTAYGHSI WINETYVGSW AGTSINDNNN 

       790        800        810        820        830        840 
ATYTLPTLQS GKNYVITVVI DNMGLDEDWT IGSEDMKNPR GIIQYSLSGQ EASAISWKLT 

       850        860        870        880        890        900 
GNLGGENYRD TVRGPLNEGG LYAERQGFHQ PQPPTQKWDS SSPFTGLTKP GIRFYSTSFD 

       910        920        930        940        950        960 
LDLPSGYDIP LYFNFGNSTS TPAAYRVQLY VNGYQYGKYV NNIGPQTSFP VPEGILNYHG 

       970        980        990       1000       1010 
TNWLALSLWA QEDNGAKLDS FELINTTPVL TSLGEVKSVN QPKYQARKGA Y 

« Hide

References

[1]"Crystal structures of beta-galactosidase from Penicillium sp. and its complex with galactose."
Rojas A.L., Nagem R.A., Neustroev K.N., Arand M., Adamska M., Eneyskaya E.V., Kulminskaya A.A., Garratt R.C., Golubev A.M., Polikarpov I.
J. Mol. Biol. 343:1281-1292(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 41-1011 IN COMPLEX WITH GALACTOSE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-374; ASN-456; ASN-625; ASN-707; ASN-763; ASN-780 AND ASN-917.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ629057 Genomic DNA. Translation: CAF32457.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TG7X-ray1.90A41-1011[»]
1XC6X-ray2.10A41-1011[»]
ProteinModelPortalQ700S9.
SMRQ700S9. Positions 41-1011.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH35. Glycoside Hydrolase Family 35.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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. 2 hits.
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...

Other

EvolutionaryTraceQ700S9.

Entry information

Entry nameBGALA_PENSQ
AccessionPrimary (citable) accession number: Q700S9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 53 of the entry and version 1 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