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A4Q8F7

- GH109_ELIME

UniProt

A4Q8F7 - GH109_ELIME

Protein

Alpha-N-acetylgalactosaminidase

Gene

nagA

Organism
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 37 (01 Oct 2014)
      Sequence version 1 (15 May 2007)
      Previous versions | rss
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    Functioni

    Glycosidase that has specific alpha-N-acetylgalactosaminidase activity.1 Publication

    Catalytic activityi

    Cleavage of non-reducing alpha-(1->3)-N-acetylgalactosamine residues from human blood group A and AB mucin glycoproteins, Forssman hapten and blood group A lacto series glycolipids.1 Publication

    Cofactori

    Binds 1 NAD+ per subunit. The NAD cannot dissociate.1 Publication

    Kineticsi

    1. KM=25.1 mM for Galalpha-pNP1 Publication
    2. KM=3.6 mM for Galbeta-pNP1 Publication
    3. KM=0.077 mM for GalNAcalpha-pNP1 Publication
    4. KM=0.23 mM for GalNAcbeta-pNP1 Publication

    pH dependencei

    Optimum pH is 6.8.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei52 – 521NAD
    Binding sitei80 – 801NAD; via carbonyl oxygen
    Binding sitei107 – 1071NAD
    Binding sitei150 – 1501NAD
    Binding sitei179 – 1791Substrate
    Binding sitei213 – 2131Substrate
    Binding sitei225 – 2251NAD
    Binding sitei307 – 3071Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi30 – 312NAD
    Nucleotide bindingi101 – 1044NAD
    Nucleotide bindingi121 – 1222NAD
    Nucleotide bindingi208 – 2125NAD

    GO - Molecular functioni

    1. alpha-N-acetylgalactosaminidase activity Source: UniProtKB-EC
    2. oxidoreductase activity Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Ligandi

    NAD

    Protein family/group databases

    CAZyiGH109. Glycoside Hydrolase Family 109.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-N-acetylgalactosaminidase (EC:3.2.1.49)
    Alternative name(s):
    Glycosyl hydrolase family 109 protein
    Gene namesi
    Name:nagA
    OrganismiElizabethkingia meningoseptica (Chryseobacterium meningosepticum)
    Taxonomic identifieri238 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeElizabethkingia

    Pathology & Biotechi

    Biotechnological usei

    Specifically cleaves the blood group A antigen at neutral pH with low consumption of recombinant enzyme. It is therefore a good candidate to participate in the development of universal red blood cells by removing blood group A antigen.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 444444Alpha-N-acetylgalactosaminidasePRO_0000348545Add
    BLAST

    Structurei

    Secondary structure

    1
    444
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi21 – 266
    Helixi30 – 4011
    Beta strandi45 – 517
    Helixi55 – 6713
    Beta strandi74 – 763
    Turni80 – 823
    Helixi83 – 864
    Beta strandi94 – 974
    Helixi101 – 1033
    Helixi104 – 11310
    Beta strandi117 – 1204
    Helixi128 – 14114
    Beta strandi145 – 1473
    Helixi150 – 1534
    Helixi155 – 16511
    Turni166 – 1694
    Beta strandi171 – 1777
    Helixi184 – 1874
    Helixi208 – 2114
    Helixi213 – 2197
    Helixi227 – 23711
    Turni240 – 2423
    Beta strandi245 – 2528
    Helixi257 – 26610
    Helixi271 – 2744
    Beta strandi283 – 2897
    Beta strandi294 – 3007
    Beta strandi312 – 3176
    Beta strandi319 – 3224
    Beta strandi324 – 3263
    Beta strandi330 – 3345
    Turni336 – 3416
    Beta strandi346 – 3483
    Helixi349 – 3546
    Helixi358 – 36710
    Helixi375 – 38915
    Helixi397 – 41519
    Turni416 – 4183
    Turni426 – 4338

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2IXAX-ray2.30A1-444[»]
    2IXBX-ray2.40A1-444[»]
    ProteinModelPortaliA4Q8F7.
    SMRiA4Q8F7. Positions 19-444.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiA4Q8F7.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni225 – 2284Substrate binding

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR016040. NAD(P)-bd_dom.
    IPR000683. Oxidoreductase_N.
    [Graphical view]
    PfamiPF01408. GFO_IDH_MocA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A4Q8F7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGALIPSSTL FNIFDFNPKK VRIAFIAVGL RGQTHVENMA RRDDVEIVAF    50
    ADPDPYMVGR AQEILKKNGK KPAKVFGNGN DDYKNMLKDK NIDAVFVSSP 100
    WEWHHEHGVA AMKAGKIVGM EVSGAITLEE CWDYVKVSEQ TGVPLMALEN 150
    VCYRRDVMAI LNMVRKGMFG ELVHGTGGYQ HDLRPVLFNS GINGKNGDGV 200
    EFGEKAFSEA KWRTNHYKNR NGELYPTHGV GPLHTMMDIN RGNRLLRLSS 250
    FASKARGLHK YIVDKGGESH PNAKVEWKQG DIVTTQIQCH NGETIVLTHD 300
    TSLQRPYNLG FKVQGTEGLW EDFGWGEAAQ GFIYFEKIMN HSHRWDSSEK 350
    WIKEYDHPMW KKHEQKAVGA GHGGMDYFLD NTFVECIKRN EAFPLDVYDL 400
    ATWYSITPLS EKSIAENGAV QEIPDFTNGK WKNAKNTFAI NDDY 444
    Length:444
    Mass (Da):50,211
    Last modified:May 15, 2007 - v1
    Checksum:i31457EDBC89518FB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM039444 Genomic DNA. Translation: CAJ01376.1.

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    The juice of life - Issue 98 of October 2008

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM039444 Genomic DNA. Translation: CAJ01376.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2IXA X-ray 2.30 A 1-444 [» ]
    2IXB X-ray 2.40 A 1-444 [» ]
    ProteinModelPortali A4Q8F7.
    SMRi A4Q8F7. Positions 19-444.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH109. Glycoside Hydrolase Family 109.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei A4Q8F7.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR016040. NAD(P)-bd_dom.
    IPR000683. Oxidoreductase_N.
    [Graphical view ]
    Pfami PF01408. GFO_IDH_MocA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, BIOTECHNOLOGY, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
      Strain: ATCC 33958.

    Entry informationi

    Entry nameiGH109_ELIME
    AccessioniPrimary (citable) accession number: A4Q8F7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 2, 2008
    Last sequence update: May 15, 2007
    Last modified: October 1, 2014
    This is version 37 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic 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. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3