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Q4ZHV7 (BGALA_ASPPH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 46. 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:
Probable beta-galactosidase A

EC=3.2.1.23
Alternative name(s):
Lactase A
Gene names
Name:lacA
OrganismAspergillus phoenicis (Aspergillus saitoi)
Taxonomic identifier5063 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length1007 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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
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 – 1818 Potential
Chain19 – 1007989Probable beta-galactosidase A
PRO_0000395219

Sites

Active site2001Proton donor Potential
Active site2981Nucleophile Potential
Binding site961Substrate By similarity
Binding site1401Substrate By similarity
Binding site1411Substrate; via amide nitrogen By similarity
Binding site1421Substrate By similarity
Binding site1991Substrate By similarity
Binding site2601Substrate By similarity
Binding site3641Substrate By similarity

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
Glycosylation9141N-linked (GlcNAc...) Potential
Disulfide bond205 ↔ 206 By similarity
Disulfide bond266 ↔ 315 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4ZHV7 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: D724DF7B1CDE94C3

FASTA1,007109,682
        10         20         30         40         50         60 
MKLSSACAIA LLAAQAAGAS IKHRINGFTL TEHSDPAKRE LLQKYVTWDD KSLFINGERI 

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

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

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

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

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

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

       430        440        450        460        470        480 
GNSTGSFFVV RHSDYSSEES TSYKLRLPTS ASSVTIPQLG GTLTLNGRDS KIHVTDYNVS 

       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 YVITVVINNM GLEENWTVGE DLMKTPRGIL NFLLAGRPSS AISWKLTGNL 

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

       910        920        930        940        950        960 
PKGWDVPLFL NIGNSTTPSP YRVQVYVNGY QYAKYISNIG PQTSFPVPEG ILNYRGTNWL 

       970        980        990       1000 
AVTLWALDSA GGKLESLELS YTTPVLTALG EVESVDQPKY KKRKGAY 

« Hide

References

[1]"The cDNA sequence of beta-galactosidase from Aspergillus phoenicis."
Wang W.K., Dong Z.Y., Mao A.J.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: AS.3.3143.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ008057 mRNA. Translation: AAY21925.1.

3D structure databases

ProteinModelPortalQ4ZHV7.
SMRQ4ZHV7. Positions 41-1007.
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...

Entry information

Entry nameBGALA_ASPPH
AccessionPrimary (citable) accession number: Q4ZHV7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: June 7, 2005
Last modified: April 16, 2014
This is version 46 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries