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Q2UCU3 (BGALA_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 56. 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
ORF Names:AO090012000445
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length1005 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
Complete proteome
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 – 1005987Probable beta-galactosidase A
PRO_0000395218

Regions

Compositional bias175 – 18410Poly-Ala

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
Glycosylation4531N-linked (GlcNAc...) Potential
Glycosylation4781N-linked (GlcNAc...) Potential
Glycosylation5221N-linked (GlcNAc...) Potential
Glycosylation6221N-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

Secondary structure

................................................................................................................................................................................. 1005
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q2UCU3 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: BAD290D2FA9EB003

FASTA1,005109,870
        10         20         30         40         50         60 
MKLLSVAAVA LLAAQAAGAS IKHRLNGFTI LEHPDPAKRD LLQDIVTWDD KSLFINGERI 

        70         80         90        100        110        120 
MLFSGEVHPF RLPVPSLWLD IFHKIRALGF NCVSFYIDWA LLEGKPGDYR AEGIFALEPF 

       130        140        150        160        170        180 
FDAAKEAGIY LIARPGSYIN AEVSGGGFPG WLQRVNGTLR SSDEPFLKAT DNYIANAAAA 

       190        200        210        220        230        240 
VAKAQITNGG PVILYQPENE YSGGCCGVKY PDADYMQYVM DQARKADIVV PFISNDASPS 

       250        260        270        280        290        300 
GHNAPGSGTG AVDIYGHDSY PLGFDCANPS VWPEGKLPDN FRTLHLEQSP STPYSLLEFQ 

       310        320        330        340        350        360 
AGAFDPWGGP GFEKCYALVN HEFSRVFYRN DLSFGVSTFN LYMTFGGTNW GNLGHPGGYT 

       370        380        390        400        410        420 
SYDYGSPITE TRNVTREKYS DIKLLANFVK ASPSYLTATP RNLTTGVYTD TSDLAVTPLI 

       430        440        450        460        470        480 
GDSPGSFFVV RHTDYSSQES TSYKLKLPTS AGNLTIPQLE GTLSLNGRDS KIHVVDYNVS 

       490        500        510        520        530        540 
GTNIIYSTAE VFTWKKFDGN KVLVLYGGPK EHHELAIASK SNVTIIEGSD SGIVSTRKGS 

       550        560        570        580        590        600 
SVIIGWDVSS TRRIVQVGDL RVFLLDRNSA YNYWVPELPT EGTSPGFSTS KTTASSIIVK 

       610        620        630        640        650        660 
AGYLLRGAHL DGADLHLTAD FNATTPIEVI GAPTGAKNLF VNGEKASHTV DKNGIWSSEV 

       670        680        690        700        710        720 
KYAAPEIKLP GLKDLDWKYL DTLPEIKSSY DDSAWVSADL PKTKNTHRPL DTPTSLYSSD 

       730        740        750        760        770        780 
YGFHTGYLIY RGHFVANGKE SEFFIRTQGG SAFGSSVWLN ETYLGSWTGA DYAMDGNSTY 

       790        800        810        820        830        840 
KLSQLESGKN YVITVVIDNL GLDENWTVGE ETMKNPRGIL SYKLSGQDAS AITWKLTGNL 

       850        860        870        880        890        900 
GGEDYQDKVR GPLNEGGLYA ERQGFHQPQP PSESWESGSP LEGLSKPGIG FYTAQFDLDL 

       910        920        930        940        950        960 
PKGWDVPLYF NFGNNTQAAR AQLYVNGYQY GKFTGNVGPQ TSFPVPEGIL NYRGTNYVAL 

       970        980        990       1000 
SLWALESDGA KLGSFELSYT TPVLTGYGNV ESPEQPKYEQ RKGAY 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP007161 Genomic DNA. Translation: BAE60622.1.
RefSeqXP_001727461.1. XM_001727409.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4IUGX-ray2.60A1-1005[»]
ProteinModelPortalQ2UCU3.
SMRQ2UCU3. Positions 41-1005.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAORAT00006026; CADAORAP00005912; CADAORAG00006026.
GeneID5987935.
KEGGaor:AOR_1_770194.

Phylogenomic databases

OMAHNAPGTG.
OrthoDBEOG7ZGXBD.

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_ASPOR
AccessionPrimary (citable) accession number: Q2UCU3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: January 24, 2006
Last modified: April 16, 2014
This is version 56 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