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A4Q8F7 (GH109_FLAME) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Alpha-N-acetylgalactosaminidase
EC=3.2.1.49
Alternative name(s):
Glycosyl hydrolase family 109 protein
Gene names
Name:nagA
OrganismFlavobacterium meningosepticum (Chryseobacterium meningosepticum) (Elizabethkingia meningoseptica)
Taxonomic identifier238 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Flavobacteriia › Flavobacteriales › Flavobacteriaceae › Elizabethkingia

Protein attributes

Sequence length444 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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. Ref.1

Cofactor

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

Biotechnological use

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. Ref.1

Sequence similarities

Belongs to the Gfo/Idh/MocA family. Glycosyl hydrolase 109 subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=25.1 mM for Galalpha-pNP Ref.1

KM=3.6 mM for Galbeta-pNP

KM=0.077 mM for GalNAcalpha-pNP

KM=0.23 mM for GalNAcbeta-pNP

pH dependence:

Optimum pH is 6.8.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 444444Alpha-N-acetylgalactosaminidase
PRO_0000348545

Regions

Nucleotide binding30 – 312NAD
Nucleotide binding101 – 1044NAD
Nucleotide binding121 – 1222NAD
Nucleotide binding208 – 2125NAD
Region225 – 2284Substrate binding

Sites

Binding site521NAD
Binding site801NAD; via carbonyl oxygen
Binding site1071NAD
Binding site1501NAD
Binding site1791Substrate
Binding site2131Substrate
Binding site2251NAD
Binding site3071Substrate

Secondary structure

1 .......................................................................... 444
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
A4Q8F7 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 31457EDBC89518FB

FASTA44450,211
        10         20         30         40         50         60 
MGALIPSSTL FNIFDFNPKK VRIAFIAVGL RGQTHVENMA RRDDVEIVAF ADPDPYMVGR 

        70         80         90        100        110        120 
AQEILKKNGK KPAKVFGNGN DDYKNMLKDK NIDAVFVSSP WEWHHEHGVA AMKAGKIVGM 

       130        140        150        160        170        180 
EVSGAITLEE CWDYVKVSEQ TGVPLMALEN VCYRRDVMAI LNMVRKGMFG ELVHGTGGYQ 

       190        200        210        220        230        240 
HDLRPVLFNS GINGKNGDGV EFGEKAFSEA KWRTNHYKNR NGELYPTHGV GPLHTMMDIN 

       250        260        270        280        290        300 
RGNRLLRLSS FASKARGLHK YIVDKGGESH PNAKVEWKQG DIVTTQIQCH NGETIVLTHD 

       310        320        330        340        350        360 
TSLQRPYNLG FKVQGTEGLW EDFGWGEAAQ GFIYFEKIMN HSHRWDSSEK WIKEYDHPMW 

       370        380        390        400        410        420 
KKHEQKAVGA GHGGMDYFLD NTFVECIKRN EAFPLDVYDL ATWYSITPLS EKSIAENGAV 

       430        440 
QEIPDFTNGK WKNAKNTFAI NDDY

« Hide

References

[1]"Bacterial glycosidases for the production of universal red blood cells."
Liu Q.P., Sulzenbacher G., Yuan H., Bennett E.P., Pietz G., Saunders K., Spence J., Nudelman E., Levery S.B., White T., Neveu J.M., Lane W.S., Bourne Y., Olsson M.L., Henrissat B., Clausen H.
Nat. Biotechnol. 25:454-464(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, BIOTECHNOLOGY, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Strain: ATCC 33958.

Web resources

Protein Spotlight

The juice of life - Issue 98 of October 2008

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM039444 Genomic DNA. Translation: CAJ01376.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IXAX-ray2.30A1-444[»]
2IXBX-ray2.40A1-444[»]
ProteinModelPortalA4Q8F7.
SMRA4Q8F7. Positions 19-444.
ModBaseSearch...

Protein family/group databases

CAZyGH109. Glycoside Hydrolase Family 109.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR016040. NAD(P)-bd_dom.
IPR000683. Oxidoreductase_N.
[Graphical view]
PfamPF01408. GFO_IDH_MocA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceA4Q8F7.

Entry information

Entry nameGH109_FLAME
AccessionPrimary (citable) accession number: A4Q8F7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: May 15, 2007
Last modified: March 6, 2013
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

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