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P29853

- BGAL_ASPNG

UniProt

P29853 - BGAL_ASPNG

Protein

Beta-galactosidase

Gene

lacA

Organism
Aspergillus niger
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 2 (01 Feb 1994)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei200 – 2001Proton donorSequence Analysis
    Active sitei298 – 2981NucleophileSequence Analysis

    GO - Molecular functioni

    1. beta-galactosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16612.

    Protein family/group databases

    CAZyiGH35. Glycoside Hydrolase Family 35.
    mycoCLAPiLAC35A_ASPNG.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-galactosidase (EC:3.2.1.23)
    Alternative name(s):
    Lactase-N
    Short name:
    Lactase
    INN: Tilactase
    Gene namesi
    Name:lacA
    OrganismiAspergillus niger
    Taxonomic identifieri5061 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    Pathology & Biotechi

    Pharmaceutical usei

    Capable of effecting hydrolysis of lactose in situ in the gastrointestinal tract of lactase-deficient subjects when given as replacement therapy at mealtime.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 1006987Beta-galactosidasePRO_0000012192Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi156 – 1561N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi373 – 3731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi402 – 4021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi422 – 4221N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi478 – 4781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi522 – 5221N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi622 – 6221N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi739 – 7391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi760 – 7601N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi777 – 7771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi805 – 8051N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PRIDEiP29853.

    Interactioni

    Structurei

    3D structure databases

    ProteinModelPortaliP29853.
    SMRiP29853. Positions 41-1006.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 35 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1874.

    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. 1 hit.
    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.

    P29853-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLSSACAIA LLAAQAAGAS IKHRINGFTL TEHSDPAKRE LLQKYVTWDD     50
    KSLFINGERI MIFSGEFHPF RLPVKELQLD IFQKVKALGF NCVSFYVDWA 100
    LVEGKPGEYR ADGIFDLEPF FDAASEAGIY LLARPGPYIN AESSGGGFPG 150
    WLQRVNGTLR SSDKAYLDAT DNYVSHVAAT IAKYQITNGG PIILYQPENE 200
    YTSGCSGVEF PDPVYMQYVE DQARNAGVVI PLINNDASAS GNNAPGTGKG 250
    AVDIYGHDSY PLGFDCANPT VWPSGDLPTN FRTLHLEQSP TTPYAIVEFQ 300
    GGSYDPWGGP GFAACSELLN NEFERVFYKN DFSFQIAIMN LYMIFGGTNW 350
    GNLGYPNGYT SYDYGSAVTE SRNITREKYS ELKLLGNFAK VSPGYLTASP 400
    GNLTTSGYAD TTDLTVTPLL GNSTGSFFVV RHSDYSSEES TSYKLRLPTS 450
    AGSVTIPQLG GTLTLNGRDS KIHVTDHNVS GTNIIYSTAE VFTWKKFADG 500
    KVLVLYGGAG EHHELAISTK SNVTVIEGSE SGISSKQTSS SVVVGWDVST 550
    TRRIIQVGDL KILLLDRNSA YNYWVPQLAT DGTSPGFSTP EKVASSIIVK 600
    AGYLVRTAYL KGSGLYLTAD FNATTSVEVI GVPSTAKNLF INGDKTSHTV 650
    DKNGIWSATV DYNAPDISLP SLKDLDWKYV DTLPEIQSSY DDSLWPAADL 700
    KQTKNTLRSL TTPTSLYSSD YGFHTGYLLY RGHFTATGNE STFAIDTQGG 750
    SAFGSSVWLN GTYLGSWTGL YANSDYNATY NLPQLQAGKT YVITVVIDNM 800
    GLEENWTVGE DLMKSPRGIS TSCLPDGQAA PISWKLTGNL GGEDYEDKVR 850
    GPLNEGGLYA ERQGFHQPEP PSQNWKSSSP LEGLSEAGIG FYSASFDLDL 900
    PKDGMSHCSS TSVTALRHPR TACRSTSTDI VCEIHKQHRT SDQLPCPRGN 950
    PELSRNELVG GDPVALDSAG GKLESLELSY TTPVLTALGE VESVDQPKYK 1000
    KRKGAY 1006
    Length:1,006
    Mass (Da):109,161
    Last modified:February 1, 1994 - v2
    Checksum:i7157B28A83805488
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti206 – 2061S → C in CAA00105. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L06037 Genomic DNA. Translation: AAA32696.1.
    S37150 mRNA. Translation: AAC60538.1.
    A00968 Unassigned DNA. Translation: CAA00105.1.
    PIRiT31685.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L06037 Genomic DNA. Translation: AAA32696.1 .
    S37150 mRNA. Translation: AAC60538.1 .
    A00968 Unassigned DNA. Translation: CAA00105.1 .
    PIRi T31685.

    3D structure databases

    ProteinModelPortali P29853.
    SMRi P29853. Positions 41-1006.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P29853.
    ChEMBLi CHEMBL4753.

    Protein family/group databases

    CAZyi GH35. Glycoside Hydrolase Family 35.
    mycoCLAPi LAC35A_ASPNG.

    Proteomic databases

    PRIDEi P29853.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG1874.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-16612.

    Family and domain databases

    Gene3Di 2.102.20.10. 1 hit.
    2.60.120.260. 2 hits.
    2.60.390.10. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR018954. 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 ]
    PANTHERi PTHR23421. PTHR23421. 1 hit.
    Pfami PF10435. BetaGal_dom2. 1 hit.
    PF13363. BetaGal_dom3. 1 hit.
    PF13364. BetaGal_dom4_5. 1 hit.
    PF01301. Glyco_hydro_35. 1 hit.
    [Graphical view ]
    PRINTSi PR00742. GLHYDRLASE35.
    SMARTi SM01029. BetaGal_dom2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF117100. SSF117100. 1 hit.
    SSF49785. SSF49785. 2 hits.
    SSF51445. SSF51445. 1 hit.
    PROSITEi PS01182. GLYCOSYL_HYDROL_F35. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Saccharomyces cerevisiae cells secreting an Aspergillus niger beta-galactosidase grow on whey permeate."
      Kumar V., Ramakrishnan S., Teeri T.T., Knowles J.K., Hartley B.S.
      Biotechnology (N.Y.) 10:82-85(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Strain: VTT D-80144.
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PHARMACEUTICAL USE.
      Strain: VTT D-80144.

    Entry informationi

    Entry nameiBGAL_ASPNG
    AccessioniPrimary (citable) accession number: P29853
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 87 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Pharmaceutical

    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