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Q0T065 (NANA_SHIF8) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 39. 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:
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:SFV_3250
OrganismShigella flexneri serotype 5b (strain 8401) [Complete proteome] [HAMAP]
Taxonomic identifier373384 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 MF_01237

Catalytic activity

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

Pathway

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

Subunit structure

Homotetramer By similarity. HAMAP MF_01237

Subcellular location

Cytoplasm By similarity HAMAP MF_01237.

Sequence similarities

Belongs to the DHDPS family. NanA subfamily.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   LigandSchiff base
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionN-acetylneuraminate lyase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 297297N-acetylneuraminate lyase HAMAP MF_01237
PRO_1000066934

Regions

Region47 – 482Substrate binding By similarity

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q0T065 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: BA9F30B4A7624167

FASTA29732,593
        10         20         30         40         50         60 
MATNLRGVMA ALLTPFDQQQ ALDKASLRRL VQFNIQQGID GLYVGGSTGE AFVQSLSERE 

        70         80         90        100        110        120 
QVLEIVAEEA KGKIKLIAHV GCVSTAESQQ LAASAKRYGF DAVSAVTPFY YPFSFEEHCD 

       130        140        150        160        170        180 
HYRAIIDSAD GLPMVVYNIP ALSGVKLTLD QINTLVTLPG VGALKQTSGD LYQMEQIRRE 

       190        200        210        220        230        240 
HPDLVLYNGY DEIFASGLLA GADGGIGSTY NIMGWRYQGI VKALKEGDIQ TAQKLQTECN 

       250        260        270        280        290 
KVIDLLIKTG VFRGLKTVLH YMDVVSVPLC RKPFGPVDEK YLPELKALAQ QLMQERG

« Hide

References

[1]"Complete genome sequence of Shigella flexneri 5b and comparison with Shigella flexneri 2a."
Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J., Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.
BMC Genomics 7:173-173(2006) [PubMed: 16822325] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 8401.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000266 Genomic DNA. Translation: ABF05300.1.
RefSeqYP_690605.1. NC_008258.1.

3D structure databases

ProteinModelPortalQ0T065.
SMRQ0T065. Positions 2-296.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0T065.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000094997; EBESCP00000091193; EBESCG00000094041.
GeneID4207664.
GenomeReviewsGene locus SFV_3250 in contig CP000266_GR.
KEGGsfv:SFV_3250.
PATRIC18730507. VBIShiFle33408_3717.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0329.
GeneTreeEBGT00050000008975.
HOGENOMHBG358848.
OMADHVIIHV.
ProtClustDBPRK04147.

Enzyme and pathway databases

BioCycSFLE373384:SFV_3250-MONOMER.

Family and domain databases

HAMAPMF_01237. N-acetylneuram_lyase.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR002220. Dihydrodipicolinate_synth-like.
IPR020625. Dihydrodipicolinate_synth_AS.
IPR020624. Dihydrodipicolinate_synth_CS.
IPR005264. NanA.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KOK01639.
PANTHERPTHR12128. DHDPS. 1 hit.
PfamPF00701. DHDPS. 1 hit.
[Graphical view]
PIRSFPIRSF001365. DHDPS. 1 hit.
PRINTSPR00146. DHPICSNTHASE.
TIGRFAMsTIGR00683. NanA. 1 hit.
PROSITEPS00665. DHDPS_1. 1 hit.
PS00666. DHDPS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNANA_SHIF8
AccessionPrimary (citable) accession number: Q0T065
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 5, 2006
Last modified: January 25, 2012
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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