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Protein

Probable beta-galactosidase E

Gene

lacE

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei92 – 921SubstrateBy similarity
Binding sitei136 – 1361SubstrateBy similarity
Binding sitei137 – 1371Substrate; via amide nitrogenBy similarity
Binding sitei138 – 1381SubstrateBy similarity
Binding sitei195 – 1951SubstrateBy similarity
Active sitei196 – 1961Proton donorSequence Analysis
Binding sitei261 – 2611SubstrateBy similarity
Active sitei299 – 2991NucleophileSequence Analysis
Binding sitei365 – 3651SubstrateBy similarity

GO - Molecular functioni

  1. beta-galactosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Names & Taxonomyi

Protein namesi
Recommended name:
Probable beta-galactosidase E (EC:3.2.1.23)
Alternative name(s):
Lactase E
Gene namesi
Name:lacE
ORF Names:AFUA_3G00380
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530 Componenti: Chromosome 3

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 1011992Probable beta-galactosidase EPRO_0000395243Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi202 – 2021N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi267 ↔ 316By similarity
Glycosylationi406 – 4061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi423 – 4231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi446 – 4461N-linked (GlcNAc...)Sequence Analysis
Glycosylationi455 – 4551N-linked (GlcNAc...)Sequence Analysis
Glycosylationi588 – 5881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi622 – 6221N-linked (GlcNAc...)Sequence Analysis
Glycosylationi704 – 7041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi745 – 7451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi759 – 7591N-linked (GlcNAc...)Sequence Analysis
Glycosylationi772 – 7721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi778 – 7781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi913 – 9131N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5085.CADAFUAP00000139.

Structurei

3D structure databases

ProteinModelPortaliQ4WG05.
SMRiQ4WG05. Positions 37-1011.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 35 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1874.
HOGENOMiHOG000181922.
InParanoidiQ4WG05.
KOiK01190.
OMAiGIDAYPM.
OrthoDBiEOG7ZGXBD.

Family and domain databases

Gene3Di2.102.20.10. 1 hit.
2.60.120.260. 2 hits.
2.60.390.10. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR018954. 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]
PANTHERiPTHR23421. PTHR23421. 1 hit.
PfamiPF10435. BetaGal_dom2. 1 hit.
PF13363. BetaGal_dom3. 1 hit.
PF13364. BetaGal_dom4_5. 2 hits.
PF01301. Glyco_hydro_35. 1 hit.
[Graphical view]
PRINTSiPR00742. GLHYDRLASE35.
SMARTiSM01029. BetaGal_dom2. 1 hit.
[Graphical view]
SUPFAMiSSF117100. SSF117100. 1 hit.
SSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEiPS01182. GLYCOSYL_HYDROL_F35. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q4WG05-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSLLKRLIA LAAAYSVAAA PSFSHHSSQD AANKRELLQD LVTWDQHSLF
60 70 80 90 100
VRGERLMIFS GEFHPFRLPV PGLWFDVFQK IKSLGFNAVS FYTDWGLMEG
110 120 130 140 150
NPGHVVTDGI WSLDEFFTAA REAGLYLIAR PGPYINAETS AGGIPGWVLR
160 170 180 190 200
RKGIIRSNSE DYLRATDTYM ATLGKIIAKA QITNGGPVIL VQPENEYTTW
210 220 230 240 250
PNVSESEFPT TMNQEVMAYA EKQLRDAGVV VPTVVNDNKN LGYFAPGTGL
260 270 280 290 300
GETDLYGIDA YPMRYDCGNP YVWPTYRFPR DWQHEHRNHS PTTPFAIMEF
310 320 330 340 350
QGGSGDGWGG VTEDGCAILV NNEAVRVVYK NNYGFGVRVF NIYMTYGGTN
360 370 380 390 400
WGNLGYYGGY TSYDYGAAIT EDRQIWREKY SEEKLQANFL KVSPAYLTST
410 420 430 440 450
PGNGVNGSYT GNKDITVTPL FGNGTTTNLY LVRHADFTST GSAQYNLSIS
460 470 480 490 500
TSVGNVTIPQ LGGSLSLNGR DSKFHITDYD VGGFNLIYSS AEVFTWAKGD
510 520 530 540 550
NKKRVLVLYG GAGELHEFAL PKHLPRPTVV EGSYVKIAKQ GSAWVVQWEV
560 570 580 590 600
AAQRRVLRAG KLEIHLLWRN DAYQHWVLEL PAKQPIANYS SPSKETVIVK
610 620 630 640 650
GGYLLRSAWI TDNDLHLTGD VNVTTPLEVI SAPKRFDGIV FNGQSLKSTR
660 670 680 690 700
SKIGNLAATV HYQPPAISLP DLKRLDWKYI DSLPEISTEY NDEGWTPLTN
710 720 730 740 750
TYTNNTREFT GPTCLYADDY GYHGGSLIYR GHFTANGDES WVFLNTSGGV
760 770 780 790 800
GFANSVWLNQ TFLGSWTGSG RNMTYPRNIS LPHELSPGEP YVFTVVIDHM
810 820 830 840 850
GQDEEAPGTD AIKFPRGILD YALSGHELSD LRWKMTGNLG GEQYQDLTRG
860 870 880 890 900
PLNEGAMYAE RQGYHLPSPP TSSWKSSNPI KEGLTGAGIG FYATSFSLDL
910 920 930 940 950
PEGYDIPLSF RFNNSASAAR SGTSYRCQLF VNGYQFGKYV NDLGPQTKFP
960 970 980 990 1000
VPEGILNYNG VNYVAVSLWA LESQGALIGG LDLVASTPIL SGYRKPAPAP
1010
QPGWKPRRGA Y
Length:1,011
Mass (Da):111,734
Last modified:July 5, 2005 - v1
Checksum:i6312E4B521800294
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000010 Genomic DNA. Translation: EAL86322.1.
RefSeqiXP_748360.1. XM_743267.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00000139; CADAFUAP00000139; CADAFUAG00000139.
GeneIDi3505787.
KEGGiafm:AFUA_3G00380.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000010 Genomic DNA. Translation: EAL86322.1.
RefSeqiXP_748360.1. XM_743267.1.

3D structure databases

ProteinModelPortaliQ4WG05.
SMRiQ4WG05. Positions 37-1011.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5085.CADAFUAP00000139.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUAT00000139; CADAFUAP00000139; CADAFUAG00000139.
GeneIDi3505787.
KEGGiafm:AFUA_3G00380.

Phylogenomic databases

eggNOGiCOG1874.
HOGENOMiHOG000181922.
InParanoidiQ4WG05.
KOiK01190.
OMAiGIDAYPM.
OrthoDBiEOG7ZGXBD.

Family and domain databases

Gene3Di2.102.20.10. 1 hit.
2.60.120.260. 2 hits.
2.60.390.10. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR018954. 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]
PANTHERiPTHR23421. PTHR23421. 1 hit.
PfamiPF10435. BetaGal_dom2. 1 hit.
PF13363. BetaGal_dom3. 1 hit.
PF13364. BetaGal_dom4_5. 2 hits.
PF01301. Glyco_hydro_35. 1 hit.
[Graphical view]
PRINTSiPR00742. GLHYDRLASE35.
SMARTiSM01029. BetaGal_dom2. 1 hit.
[Graphical view]
SUPFAMiSSF117100. SSF117100. 1 hit.
SSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEiPS01182. GLYCOSYL_HYDROL_F35. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Entry informationi

Entry nameiBGALE_ASPFU
AccessioniPrimary (citable) accession number: Q4WG05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: July 5, 2005
Last modified: January 7, 2015
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.