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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)DescriptionActionsGraphical viewLength
    Binding sitei52NAD1
    Binding sitei80NAD; via carbonyl oxygen1
    Binding sitei107NAD1
    Binding sitei150NAD1
    Binding sitei179Substrate1
    Binding sitei213Substrate1
    Binding sitei225NAD1
    Binding sitei307Substrate1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi30 – 31NAD2
    Nucleotide bindingi101 – 104NAD4
    Nucleotide bindingi121 – 122NAD2
    Nucleotide bindingi208 – 212NAD5

    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)DescriptionActionsGraphical viewLength
    ChainiPRO_00003485451 – 444Alpha-N-acetylgalactosaminidaseAdd BLAST444

    Structurei

    Secondary structure

    1444
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi21 – 26Combined sources6
    Helixi30 – 40Combined sources11
    Beta strandi45 – 51Combined sources7
    Helixi55 – 67Combined sources13
    Beta strandi74 – 76Combined sources3
    Turni80 – 82Combined sources3
    Helixi83 – 86Combined sources4
    Beta strandi94 – 97Combined sources4
    Helixi101 – 103Combined sources3
    Helixi104 – 113Combined sources10
    Beta strandi117 – 120Combined sources4
    Helixi128 – 141Combined sources14
    Beta strandi145 – 147Combined sources3
    Helixi150 – 153Combined sources4
    Helixi155 – 165Combined sources11
    Turni166 – 169Combined sources4
    Beta strandi171 – 177Combined sources7
    Helixi184 – 187Combined sources4
    Helixi208 – 211Combined sources4
    Helixi213 – 219Combined sources7
    Helixi227 – 237Combined sources11
    Turni240 – 242Combined sources3
    Beta strandi245 – 252Combined sources8
    Helixi257 – 266Combined sources10
    Helixi271 – 274Combined sources4
    Beta strandi283 – 289Combined sources7
    Beta strandi294 – 300Combined sources7
    Beta strandi312 – 317Combined sources6
    Beta strandi319 – 322Combined sources4
    Beta strandi324 – 326Combined sources3
    Beta strandi330 – 334Combined sources5
    Turni336 – 341Combined sources6
    Beta strandi346 – 348Combined sources3
    Helixi349 – 354Combined sources6
    Helixi358 – 367Combined sources10
    Helixi375 – 389Combined sources15
    Helixi397 – 415Combined sources19
    Turni416 – 418Combined sources3
    Turni426 – 433Combined sources8

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiA4Q8F7.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni225 – 228Substrate binding4

    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]
    SUPFAMiSSF51735. SSF51735. 1 hit.

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2IXAX-ray2.30A1-444[»]
    2IXBX-ray2.40A1-444[»]
    ProteinModelPortaliA4Q8F7.
    SMRiA4Q8F7.
    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]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    ProtoNetiSearch...

    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: November 2, 2016
    This is version 46 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

    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 one 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.