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Q2G160 (NANA_STAA8) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-acetylneuraminate lyase

EC=4.1.3.3
Alternative name(s):
N-acetylneuraminate pyruvate-lyase
N-acetylneuraminic acid aldolase
Sialate lyase
Sialic acid aldolase
Sialic acid lyase
Gene names
Name:nanA
Ordered Locus Names:SAOUHSC_00295
OrganismStaphylococcus aureus (strain NCTC 8325) [Reference proteome] [HAMAP]
Taxonomic identifier93061 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length293 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate By similarity. HAMAP-Rule MF_01237

Catalytic activity

N-acetylneuraminate = N-acetyl-D-mannosamine + pyruvate. HAMAP-Rule MF_01237

Pathway

Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 1/5. HAMAP-Rule MF_01237

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_01237

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01237.

Sequence similarities

Belongs to the DapA family. NanA subfamily.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   LigandSchiff base
   Molecular functionLyase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processN-acetylneuraminate catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

carbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionN-acetylneuraminate lyase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 293293N-acetylneuraminate lyase HAMAP-Rule MF_01237
PRO_1000066938

Regions

Region48 – 492Substrate binding By similarity

Sites

Active site1651Schiff-base intermediate with substrate By similarity
Site1371Involved in proton transfer during cleavage By similarity

Secondary structure

............................................... 293
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q2G160 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 62D7DEFFDC1AF431

FASTA29333,043
        10         20         30         40         50         60 
MNKDLKGLYA ALLVPFDENG QVNEQGLKQI AQNAIETEEL DGLYVNGSSG ENFLLNTEQK 

        70         80         90        100        110        120 
KQVFKVAKEA VGDKVKLIAQ VGSLDLNEAI ELGKYATELG YDALSAVTPF YYPFTFEEIR 

       130        140        150        160        170        180 
DYYFDIIEAT QNNMIIYAIP DLTGVNISIE QFSELFNHEK IVGVKYTAPN FFLLERIRKA 

       190        200        210        220        230        240 
FPDKLILSGF DEMLVQATIS GVDGAIGSTY NVNGRRARKI FDLARQGQIQ EAYQLQHDSN 

       250        260        270        280        290 
DIIETVLSMG IYPTLKEILR HRGIDAGLPK RPFKPFNEAH RQTLDQLIAK YDL 

« Hide

References

[1]"The Staphylococcus aureus NCTC 8325 genome."
Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.
(In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.); Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington D.C. (2006)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 8325.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000253 Genomic DNA. Translation: ABD29464.1.
RefSeqYP_498885.1. NC_007795.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4AH7X-ray2.30A/B/C/D2-293[»]
4AHOX-ray2.00A/B/C/D1-293[»]
4AHPX-ray2.10A/B/C/D2-293[»]
4AHQX-ray1.95A/B/C/D2-293[»]
4AMAX-ray2.35A/B/C/D2-293[»]
ProteinModelPortalQ2G160.
SMRQ2G160. Positions 2-293.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING93061.SAOUHSC_00295.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD29464; ABD29464; SAOUHSC_00295.
GeneID3918976.
KEGGsao:SAOUHSC_00295.
PATRIC19578184. VBIStaAur99865_0268.

Phylogenomic databases

eggNOGCOG0329.
HOGENOMHOG000173608.
KOK01639.
OMAELVPSDM.
OrthoDBEOG6W7235.

Enzyme and pathway databases

BioCycSAUR93061:GIWJ-279-MONOMER.
UniPathwayUPA00629; UER00680.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01237. N_acetylneuram_lyase.
InterProIPR013785. Aldolase_TIM.
IPR002220. DapA-like.
IPR020625. Dihydrodipicolinate_synth_AS.
IPR005264. NanA.
[Graphical view]
PANTHERPTHR12128. PTHR12128. 1 hit.
PfamPF00701. DHDPS. 1 hit.
[Graphical view]
PIRSFPIRSF001365. DHDPS. 1 hit.
PRINTSPR00146. DHPICSNTHASE.
PROSITEPS00666. DHDPS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNANA_STAA8
AccessionPrimary (citable) accession number: Q2G160
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: March 21, 2006
Last modified: July 9, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways