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Q700S9

- BGALA_PENSQ

UniProt

Q700S9 - BGALA_PENSQ

Protein

Probable beta-galactosidase A

Gene

lacA

Organism
Penicillium sp.
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 54 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    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 sitei96 – 961Substrate
    Binding sitei140 – 1401Substrate
    Binding sitei141 – 1411Substrate; via amide nitrogen
    Binding sitei142 – 1421Substrate
    Binding sitei199 – 1991Substrate
    Active sitei200 – 2001Proton donorSequence Analysis
    Binding sitei261 – 2611Substrate
    Active sitei299 – 2991NucleophileSequence Analysis
    Binding sitei365 – 3651Substrate

    GO - Molecular functioni

    1. beta-galactosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. polysaccharide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation

    Protein family/group databases

    CAZyiGH35. Glycoside Hydrolase Family 35.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable beta-galactosidase A (EC:3.2.1.23)
    Alternative name(s):
    Lactase A
    Gene namesi
    Name:lacA
    OrganismiPenicillium sp.
    Taxonomic identifieri5081 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 1011992Probable beta-galactosidase APRO_5000072460Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi205 ↔ 2061 Publication
    Disulfide bondi267 ↔ 3161 Publication
    Glycosylationi374 – 3741N-linked (GlcNAc...)1 Publication
    Glycosylationi456 – 4561N-linked (GlcNAc...)1 Publication
    Glycosylationi625 – 6251N-linked (GlcNAc...)1 Publication
    Glycosylationi707 – 7071N-linked (GlcNAc...)1 Publication
    Glycosylationi763 – 7631N-linked (GlcNAc...)1 Publication
    Glycosylationi780 – 7801N-linked (GlcNAc...)1 Publication
    Glycosylationi917 – 9171N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Structurei

    Secondary structure

    1
    1011
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi44 – 485
    Beta strandi53 – 553
    Beta strandi58 – 603
    Beta strandi62 – 665
    Helixi69 – 713
    Helixi75 – 773
    Helixi78 – 869
    Turni87 – 893
    Beta strandi92 – 965
    Helixi99 – 1024
    Helixi113 – 1153
    Helixi118 – 12710
    Beta strandi130 – 1345
    Helixi144 – 1474
    Helixi150 – 1545
    Helixi164 – 18320
    Helixi186 – 1883
    Beta strandi190 – 1956
    Helixi214 – 22613
    Beta strandi237 – 2415
    Beta strandi257 – 2604
    Helixi282 – 2898
    Beta strandi296 – 3038
    Helixi313 – 3197
    Helixi322 – 33312
    Turni334 – 3363
    Beta strandi338 – 3436
    Helixi378 – 39114
    Helixi394 – 3974
    Beta strandi399 – 4013
    Beta strandi405 – 4117
    Beta strandi415 – 4217
    Beta strandi429 – 4379
    Beta strandi444 – 4463
    Beta strandi448 – 4525
    Beta strandi455 – 4595
    Beta strandi461 – 4644
    Beta strandi466 – 4683
    Beta strandi474 – 4829
    Beta strandi485 – 50016
    Beta strandi503 – 5108
    Beta strandi515 – 5217
    Beta strandi527 – 5315
    Beta strandi537 – 5415
    Beta strandi544 – 5507
    Beta strandi556 – 5605
    Beta strandi563 – 5697
    Helixi570 – 5734
    Beta strandi583 – 5864
    Helixi593 – 5975
    Beta strandi601 – 6033
    Beta strandi605 – 61410
    Beta strandi617 – 62610
    Beta strandi628 – 6347
    Beta strandi641 – 6444
    Beta strandi647 – 6493
    Beta strandi659 – 6635
    Helixi675 – 6773
    Beta strandi681 – 6855
    Helixi687 – 6893
    Beta strandi698 – 7003
    Beta strandi714 – 7174
    Helixi721 – 7244
    Beta strandi731 – 7388
    Beta strandi745 – 7517
    Beta strandi758 – 7625
    Beta strandi765 – 7706
    Beta strandi777 – 7848
    Beta strandi793 – 8008
    Helixi815 – 8173
    Beta strandi821 – 8277
    Helixi832 – 8343
    Beta strandi836 – 8427
    Turni843 – 8464
    Turni851 – 8533
    Beta strandi855 – 8573
    Helixi862 – 8654
    Turni866 – 8694
    Beta strandi870 – 8723
    Turni883 – 8853
    Beta strandi887 – 90014
    Beta strandi911 – 9155
    Beta strandi925 – 9317
    Beta strandi934 – 9407
    Turni941 – 9433
    Beta strandi948 – 9514
    Beta strandi960 – 97011
    Beta strandi981 – 9855

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TG7X-ray1.90A41-1011[»]
    1XC6X-ray2.10A41-1011[»]
    ProteinModelPortaliQ700S9.
    SMRiQ700S9. Positions 41-1011.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ700S9.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 35 family.Curated

    Keywords - Domaini

    Signal

    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.

    Q700S9-1 [UniParc]FASTAAdd to Basket

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    MKLLSSWVVA ALAAQAAGAA ISHKLDGFTI REHADPAKRA LLQKYVTWDE     50
    HSIFVNGERL MIFSGEVHPY RLPVASLYID IFEKVKALGF NCVSFYVDWA 100
    LLEGNPGHYS AEGIFDLQPF FDAAKEAGIY LLARPGPYIN AEVSGGGFPG 150
    WLQRVDGILR TSDEAYLKAT DNYASNIAAT IAKAQITNGG PIILYQPENE 200
    YSGACCGYNG FPDGSYMQYI EDHARDAGIV VPFISNDAWA AGHNAPGTGA 250
    GAVDIYGHDS YPLGFDCANP STWPSGNLPT YFHTSHEQQS PSTPYSLVEF 300
    QGGAFDPWGG VGFAKCAALL NHEFERVFYK NDFSFGVAFL NLYMIFGGTN 350
    WGNLGHPGGY TSYDYGSAIS ESRNITREKY SELKLLGNFA KVSPGYLVAN 400
    PGDLSTSTYT NTADLTVTPL LGSNSSASSF FVIRHSDYSS QASVEYKLTV 450
    PTSAGNLTIP QLGGSLTLSG RDSKIHVTDY DVAGTNILYS TAEVFTWKKF 500
    NNEKVLVLYG GPGEHHEFAV SGASSSSVVE GSSSGISSKK VGKALVVAWD 550
    VSTARRIVQV GSLKVFLLDR NSAYNYWVPQ VPTKGTAPGY SNQETTASSI 600
    IVKAGYLVRS AYLDGNDLHI QADFNATTPI EVVGAPSGAK NLVINGKKTQ 650
    TKVDKNGIWS ASVAYTAPKV QLPSLKSLKW KSVDTLPEAK NTYDDSAWTS 700
    ADHAYTNNSA HSLQTPTSLF ASDYGYHTGA LLFRGHFTAN GKEKTFFVQT 750
    KGGTAYGHSI WINETYVGSW AGTSINDNNN ATYTLPTLQS GKNYVITVVI 800
    DNMGLDEDWT IGSEDMKNPR GIIQYSLSGQ EASAISWKLT GNLGGENYRD 850
    TVRGPLNEGG LYAERQGFHQ PQPPTQKWDS SSPFTGLTKP GIRFYSTSFD 900
    LDLPSGYDIP LYFNFGNSTS TPAAYRVQLY VNGYQYGKYV NNIGPQTSFP 950
    VPEGILNYHG TNWLALSLWA QEDNGAKLDS FELINTTPVL TSLGEVKSVN 1000
    QPKYQARKGA Y 1011
    Length:1,011
    Mass (Da):109,750
    Last modified:July 5, 2004 - v1
    Checksum:iA8A5BD48354F791A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ629057 Genomic DNA. Translation: CAF32457.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ629057 Genomic DNA. Translation: CAF32457.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TG7 X-ray 1.90 A 41-1011 [» ]
    1XC6 X-ray 2.10 A 41-1011 [» ]
    ProteinModelPortali Q700S9.
    SMRi Q700S9. Positions 41-1011.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH35. Glycoside Hydrolase Family 35.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q700S9.

    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. 2 hits.
    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. "Crystal structures of beta-galactosidase from Penicillium sp. and its complex with galactose."
      Rojas A.L., Nagem R.A., Neustroev K.N., Arand M., Adamska M., Eneyskaya E.V., Kulminskaya A.A., Garratt R.C., Golubev A.M., Polikarpov I.
      J. Mol. Biol. 343:1281-1292(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 41-1011 IN COMPLEX WITH GALACTOSE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-374; ASN-456; ASN-625; ASN-707; ASN-763; ASN-780 AND ASN-917.

    Entry informationi

    Entry nameiBGALA_PENSQ
    AccessioniPrimary (citable) accession number: Q700S9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 13, 2010
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 54 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

    3D-structure

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3