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Q2UMD5 (BGALC_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 58. 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 C

EC=3.2.1.23
Alternative name(s):
Lactase C
Gene names
Name:lacC
ORF Names:AO090003000042
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length984 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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 termComplete 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 – 2323 Potential
Chain24 – 984961Probable beta-galactosidase C
PRO_0000395238

Sites

Active site1881Proton donor Potential
Active site2871Nucleophile Potential
Binding site821Substrate By similarity
Binding site1271Substrate By similarity
Binding site1281Substrate; via amide nitrogen By similarity
Binding site1291Substrate By similarity
Binding site1871Substrate By similarity
Binding site2511Substrate By similarity
Binding site3531Substrate By similarity

Amino acid modifications

Glycosylation1971N-linked (GlcNAc...) Potential
Glycosylation2761N-linked (GlcNAc...) Potential
Glycosylation3911N-linked (GlcNAc...) Potential
Glycosylation4211N-linked (GlcNAc...) Potential
Glycosylation4341N-linked (GlcNAc...) Potential
Glycosylation5171N-linked (GlcNAc...) Potential
Glycosylation6021N-linked (GlcNAc...) Potential
Glycosylation6771N-linked (GlcNAc...) Potential
Glycosylation7151N-linked (GlcNAc...) Potential
Glycosylation7201N-linked (GlcNAc...) Potential
Glycosylation7591N-linked (GlcNAc...) Potential
Glycosylation8051N-linked (GlcNAc...) Potential
Disulfide bond257 ↔ 304 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2UMD5 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 8326D1E294ACDECE

FASTA984108,653
        10         20         30         40         50         60 
MRLLSFIYLV WLALLTGTPQ VSATDNGKTS DVAWDKYSLS VKGERLFVFS GEFHYQRLPV 

        70         80         90        100        110        120 
PELWLDVFQK LRANGFNTIS VYFFWSYHSA SEDVFDFTTG AHDIQRLFDY AKQAGLYVIA 

       130        140        150        160        170        180 
RAGPYCNAET SAGGFALWAA NGQMGSERTS DEAYYKKWKP WILEVGKIIA ANQITNGGPV 

       190        200        210        220        230        240 
ILNQHENELQ ETTYDSNDTK VIYMEQVAKA FEEAGVVVPS SHNEKGMRTV SWSTDYKNVG 

       250        260        270        280        290        300 
GAVNVYGLDS YPGSLSCANP NSGFNLLRTY YQWFQNYSYT QPEYLAEFEG GWFQPWGGSF 

       310        320        330        340        350        360 
YDSCASELSP EFADVYYKNN IGSRVTLHNI YMTFGGTNWG HSAAPVVYTS YDYGSPLRET 

       370        380        390        400        410        420 
REIRDKLKQT KLLGLFTRVS KDLLKTYMEG NGTSYTSDDS IYTWALRNPD SDAGFYVVAH 

       430        440        450        460        470        480 
NTSSSREVTT FSLNITTSAG AMTIPDIELD GRQSKIIVTD YSIGSESSLL YSSAEVLTYA 

       490        500        510        520        530        540 
TLDVDVLVFY LNAGQKGAFV FKDAPADLKY QTYGNSNLSA LETSQGTQYS YTQGEGVTAV 

       550        560        570        580        590        600 
KFSNGVLVYL LDKETAWNFF APPTVSSPTV APNEHILVFG PYLVRGASIK HDTVEIVGDN 

       610        620        630        640        650        660 
SNSTSIEIYT GDEHVKKVSW NGNLIDTRAT AYGSLIGTVP GAEDIEISLP SLSSWKAQDT 

       670        680        690        700        710        720 
LPEISPDYDD SRWTICNKTT SVNSVAPLSL PVLYSGDYGY HTGTKIYRGR FDGQNATGAN 

       730        740        750        760        770        780 
VTVQNGVAAG WAAWLNGAYV GGFSGDPDKV ASWEVLKFNH SSLRSRDNVL TIITDYTGHD 

       790        800        810        820        830        840 
QNSQKPIGTQ NPRGIMGATL IGGGNFTLWR IQGNAGGEKN IDPVRGPMNE GGLYGERMGW 

       850        860        870        880        890        900 
HLPGYQVPES ALDSSPLEGV SGAEGRFYTT SFQLDLEEDL DVPIGLQLSA PAGTEAVVQI 

       910        920        930        940        950        960 
FMNGYQFGHY LPHIGPQSLF PFPPGVIKNR GQNSLAISMW ALTDAGARLE QVELKAYAKY 

       970        980 
RSGFDFNRDW TYLQPGWKDR TEYA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP007155 Genomic DNA. Translation: BAE57280.1.
RefSeqXP_001819282.1. XM_001819230.1.

3D structure databases

ProteinModelPortalQ2UMD5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5062.CADAORAP00000714.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAORAT00000727; CADAORAP00000714; CADAORAG00000727.
GeneID5991265.
KEGGaor:AOR_1_74154.

Phylogenomic databases

eggNOGCOG1874.
HOGENOMHOG000181922.
OMASGEFHYQ.
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.
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.
ProtoNetSearch...

Entry information

Entry nameBGALC_ASPOR
AccessionPrimary (citable) accession number: Q2UMD5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: January 24, 2006
Last modified: April 16, 2014
This is version 58 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