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A4Q8G1 (GH109_BACFO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismBacteroides forsythus (Tannerella forsythensis)
Taxonomic identifier28112 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Porphyromonadaceae › Tannerella

Protein attributes

Sequence length468 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Glycosidase that has specific alpha-N-acetylgalactosaminidase activity.

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 By similarity.

Post-translational modification

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.

Sequence similarities

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

Ontologies

Keywords
   DomainSignal
   LigandNAD
   Molecular functionGlycosidase
Hydrolase
Gene Ontology (GO)
   Biological_processoxidation-reduction process

Inferred from electronic annotation. Source: GOC

   Molecular_functionalpha-N-acetylgalactosaminidase activity

Inferred from electronic annotation. Source: EC

oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030Tat-type signal Potential
Chain31 – 468438Alpha-N-acetylgalactosaminidase
PRO_0000348548

Regions

Nucleotide binding62 – 632NAD By similarity
Nucleotide binding133 – 1364NAD By similarity
Nucleotide binding154 – 1552NAD By similarity
Nucleotide binding243 – 2475NAD By similarity
Region260 – 2634Substrate binding By similarity

Sites

Binding site841NAD By similarity
Binding site1831NAD By similarity
Binding site2121Substrate By similarity
Binding site2481Substrate By similarity
Binding site2601NAD By similarity
Binding site3421Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A4Q8G1 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 582356F5CE376FE2

FASTA46851,923
        10         20         30         40         50         60 
MENTRRNFLK KVTAAGIGAA GLAVTDQAMA AVNQPGEAAQ QKKKPAGKSD GMLRFGFIGT 

        70         80         90        100        110        120 
GSRCQEHINN VLGIQGNKIV AICDIQKGPL EKTLKHIAKF NVPEPKVYTG GEREFEKMLN 

       130        140        150        160        170        180 
NEEFDCVIIA SPWEWHVPMA VAAMKAGVPY VGVEVSAANT VEECWDLVNV SEATGSHLNI 

       190        200        210        220        230        240 
LENVCYRRDV MAALRMVREG LFGEMIHGTC GYQHDLRDVK FNDGIHYTYQ EGGELRMGPT 

       250        260        270        280        290        300 
AYAEAQWRTQ HSVTRNGDIY PTHGIGPVAN CLNINRGNRF LSLTSMATQS RGLHNFVVDK 

       310        320        330        340        350        360 
GGANHPYAKI HFNLGDIVTS MIKCANGQTV IVTHDTNLPR PYSLGFRIQG TRGLWMNDGN 

       370        380        390        400        410        420 
HVYVEGQSKP HRWDASDDWF KKYDHKLWST LELKAKEAGH GGMDYIMMYD FIDAIRNKKP 

       430        440        450        460 
TPMDCYDAAA WSAISGLSEM SIARGGAVVD FPDFTRGQWI HRQPAFAL

« 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], ENZYME ACTIVITY.
Strain: ATCC 43037 / JCM 10827 / FDC 338 / CIP 105219.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM039448 Genomic DNA. Translation: CAJ01380.1.

3D structure databases

ProteinModelPortalA4Q8G1.
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.
IPR006311. TAT_signal.
IPR019546. TAT_signal_bac_arc.
[Graphical view]
PfamPF01408. GFO_IDH_MocA. 1 hit.
[Graphical view]
TIGRFAMsTIGR01409. TAT_signal_seq. 1 hit.
PROSITEPS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGH109_BACFO
AccessionPrimary (citable) accession number: A4Q8G1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: May 15, 2007
Last modified: May 29, 2013
This is version 32 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

SIMILARITY comments

Index of protein domains and families

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