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Protein

Alpha-N-acetylgalactosaminidase

Gene

nagA

Organism
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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

NAD(+)1 PublicationNote: 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

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BRENDAi3.2.1.49. 1374.

    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 – 266Combined sources
    Helixi30 – 4011Combined sources
    Beta strandi45 – 517Combined sources
    Helixi55 – 6713Combined sources
    Beta strandi74 – 763Combined sources
    Turni80 – 823Combined sources
    Helixi83 – 864Combined sources
    Beta strandi94 – 974Combined sources
    Helixi101 – 1033Combined sources
    Helixi104 – 11310Combined sources
    Beta strandi117 – 1204Combined sources
    Helixi128 – 14114Combined sources
    Beta strandi145 – 1473Combined sources
    Helixi150 – 1534Combined sources
    Helixi155 – 16511Combined sources
    Turni166 – 1694Combined sources
    Beta strandi171 – 1777Combined sources
    Helixi184 – 1874Combined sources
    Helixi208 – 2114Combined sources
    Helixi213 – 2197Combined sources
    Helixi227 – 23711Combined sources
    Turni240 – 2423Combined sources
    Beta strandi245 – 2528Combined sources
    Helixi257 – 26610Combined sources
    Helixi271 – 2744Combined sources
    Beta strandi283 – 2897Combined sources
    Beta strandi294 – 3007Combined sources
    Beta strandi312 – 3176Combined sources
    Beta strandi319 – 3224Combined sources
    Beta strandi324 – 3263Combined sources
    Beta strandi330 – 3345Combined sources
    Turni336 – 3416Combined sources
    Beta strandi346 – 3483Combined sources
    Helixi349 – 3546Combined sources
    Helixi358 – 36710Combined sources
    Helixi375 – 38915Combined sources
    Helixi397 – 41519Combined sources
    Turni416 – 4183Combined sources
    Turni426 – 4338Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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

            10         20         30         40         50
    MGALIPSSTL FNIFDFNPKK VRIAFIAVGL RGQTHVENMA RRDDVEIVAF
    60 70 80 90 100
    ADPDPYMVGR AQEILKKNGK KPAKVFGNGN DDYKNMLKDK NIDAVFVSSP
    110 120 130 140 150
    WEWHHEHGVA AMKAGKIVGM EVSGAITLEE CWDYVKVSEQ TGVPLMALEN
    160 170 180 190 200
    VCYRRDVMAI LNMVRKGMFG ELVHGTGGYQ HDLRPVLFNS GINGKNGDGV
    210 220 230 240 250
    EFGEKAFSEA KWRTNHYKNR NGELYPTHGV GPLHTMMDIN RGNRLLRLSS
    260 270 280 290 300
    FASKARGLHK YIVDKGGESH PNAKVEWKQG DIVTTQIQCH NGETIVLTHD
    310 320 330 340 350
    TSLQRPYNLG FKVQGTEGLW EDFGWGEAAQ GFIYFEKIMN HSHRWDSSEK
    360 370 380 390 400
    WIKEYDHPMW KKHEQKAVGA GHGGMDYFLD NTFVECIKRN EAFPLDVYDL
    410 420 430 440
    ATWYSITPLS EKSIAENGAV QEIPDFTNGK WKNAKNTFAI NDDY
    Length:444
    Mass (Da):50,211
    Last modified:May 15, 2007 - v1
    Checksum:i31457EDBC89518FB
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AM039444 Genomic DNA. Translation: CAJ01376.1.

    3D structure databases

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

    Protein family/group databases

    CAZyiGH109. Glycoside Hydrolase Family 109.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BRENDAi3.2.1.49. 1374.

    Miscellaneous databases

    EvolutionaryTraceiA4Q8F7.

    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]
    ProtoNetiSearch...

    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: April 1, 2015
    This is version 40 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

    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.