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Q4WG05 (BGALE_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 67. 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 E

EC=3.2.1.23
Alternative name(s):
Lactase E
Gene names
Name:lacE
ORF Names:AFUA_3G00380
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length1011 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
Reference 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 – 1919 Potential
Chain20 – 1011992Probable beta-galactosidase E
PRO_0000395243

Sites

Active site1961Proton donor Potential
Active site2991Nucleophile Potential
Binding site921Substrate By similarity
Binding site1361Substrate By similarity
Binding site1371Substrate; via amide nitrogen By similarity
Binding site1381Substrate By similarity
Binding site1951Substrate By similarity
Binding site2611Substrate By similarity
Binding site3651Substrate By similarity

Amino acid modifications

Glycosylation2021N-linked (GlcNAc...) Potential
Glycosylation4061N-linked (GlcNAc...) Potential
Glycosylation4231N-linked (GlcNAc...) Potential
Glycosylation4461N-linked (GlcNAc...) Potential
Glycosylation4551N-linked (GlcNAc...) Potential
Glycosylation5881N-linked (GlcNAc...) Potential
Glycosylation6221N-linked (GlcNAc...) Potential
Glycosylation7041N-linked (GlcNAc...) Potential
Glycosylation7451N-linked (GlcNAc...) Potential
Glycosylation7591N-linked (GlcNAc...) Potential
Glycosylation7721N-linked (GlcNAc...) Potential
Glycosylation7781N-linked (GlcNAc...) Potential
Glycosylation9131N-linked (GlcNAc...) Potential
Disulfide bond267 ↔ 316 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4WG05 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 6312E4B521800294

FASTA1,011111,734
        10         20         30         40         50         60 
MKSLLKRLIA LAAAYSVAAA PSFSHHSSQD AANKRELLQD LVTWDQHSLF VRGERLMIFS 

        70         80         90        100        110        120 
GEFHPFRLPV PGLWFDVFQK IKSLGFNAVS FYTDWGLMEG NPGHVVTDGI WSLDEFFTAA 

       130        140        150        160        170        180 
REAGLYLIAR PGPYINAETS AGGIPGWVLR RKGIIRSNSE DYLRATDTYM ATLGKIIAKA 

       190        200        210        220        230        240 
QITNGGPVIL VQPENEYTTW PNVSESEFPT TMNQEVMAYA EKQLRDAGVV VPTVVNDNKN 

       250        260        270        280        290        300 
LGYFAPGTGL GETDLYGIDA YPMRYDCGNP YVWPTYRFPR DWQHEHRNHS PTTPFAIMEF 

       310        320        330        340        350        360 
QGGSGDGWGG VTEDGCAILV NNEAVRVVYK NNYGFGVRVF NIYMTYGGTN WGNLGYYGGY 

       370        380        390        400        410        420 
TSYDYGAAIT EDRQIWREKY SEEKLQANFL KVSPAYLTST PGNGVNGSYT GNKDITVTPL 

       430        440        450        460        470        480 
FGNGTTTNLY LVRHADFTST GSAQYNLSIS TSVGNVTIPQ LGGSLSLNGR DSKFHITDYD 

       490        500        510        520        530        540 
VGGFNLIYSS AEVFTWAKGD NKKRVLVLYG GAGELHEFAL PKHLPRPTVV EGSYVKIAKQ 

       550        560        570        580        590        600 
GSAWVVQWEV AAQRRVLRAG KLEIHLLWRN DAYQHWVLEL PAKQPIANYS SPSKETVIVK 

       610        620        630        640        650        660 
GGYLLRSAWI TDNDLHLTGD VNVTTPLEVI SAPKRFDGIV FNGQSLKSTR SKIGNLAATV 

       670        680        690        700        710        720 
HYQPPAISLP DLKRLDWKYI DSLPEISTEY NDEGWTPLTN TYTNNTREFT GPTCLYADDY 

       730        740        750        760        770        780 
GYHGGSLIYR GHFTANGDES WVFLNTSGGV GFANSVWLNQ TFLGSWTGSG RNMTYPRNIS 

       790        800        810        820        830        840 
LPHELSPGEP YVFTVVIDHM GQDEEAPGTD AIKFPRGILD YALSGHELSD LRWKMTGNLG 

       850        860        870        880        890        900 
GEQYQDLTRG PLNEGAMYAE RQGYHLPSPP TSSWKSSNPI KEGLTGAGIG FYATSFSLDL 

       910        920        930        940        950        960 
PEGYDIPLSF RFNNSASAAR SGTSYRCQLF VNGYQFGKYV NDLGPQTKFP VPEGILNYNG 

       970        980        990       1000       1010 
VNYVAVSLWA LESQGALIGG LDLVASTPIL SGYRKPAPAP QPGWKPRRGA Y 

« Hide

References

[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHF01000010 Genomic DNA. Translation: EAL86322.1.
RefSeqXP_748360.1. XM_743267.1.

3D structure databases

ProteinModelPortalQ4WG05.
SMRQ4WG05. Positions 37-1011.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00000139.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00000139; CADAFUAP00000139; CADAFUAG00000139.
GeneID3505787.
KEGGafm:AFUA_3G00380.

Phylogenomic databases

eggNOGCOG1874.
HOGENOMHOG000181922.
KOK01190.
OMAGIDAYPM.
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 nameBGALE_ASPFU
AccessionPrimary (citable) accession number: Q4WG05
Entry history
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: July 5, 2005
Last modified: May 14, 2014
This is version 67 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