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Q5ZKD4 (NPL_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Short name=NALase
EC=4.1.3.3
Alternative name(s):
N-acetylneuraminate pyruvate-lyase
N-acetylneuraminic acid aldolase
Sialate lyase
Sialate-pyruvate lyase
Sialic acid aldolase
Sialic acid lyase
Gene names
Name:NPL
ORF Names:RCJMB04_11j23
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length308 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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. It prevents sialic acids from being recycled and returning to the cell surface. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway By similarity.

Catalytic activity

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

Pathway

Amino-sugar metabolism; N-acetylneuraminate degradation.

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the DapA family. NanA subfamily.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   LigandSchiff base
   Molecular functionLyase
   Technical termComplete 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-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionN-acetylneuraminate lyase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 308308N-acetylneuraminate lyase
PRO_0000273357

Regions

Region50 – 512Substrate binding By similarity

Sites

Active site1721Schiff-base intermediate with substrate By similarity
Site1421Involved in proton transfer during cleavage By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5ZKD4 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: FBA9375250252359

FASTA30833,646
        10         20         30         40         50         60 
MTPRKKLEGL VAATVTPMTP DGRINLSVIH QYVDYLVSEQ NVKNIFVNGT TGEGLSLSIQ 

        70         80         90        100        110        120 
ERKQLAEEWM CQGKGKLDHV IIHVGALSLL ESQELARHAA AIGASGIAVI APSFFKPTNK 

       130        140        150        160        170        180 
DELLGFLQKV ASEAPTVPFY YYHIPAMTGV KIRVEELLDG IREQIPTFQG VKFSDTDLLD 

       190        200        210        220        230        240 
LAQCINKKER EQFVFLYGVD EQLLSALAIG ANGAVGSTYN YLGRKTNLML QAFAKPDLAL 

       250        260        270        280        290        300 
ARKYQFLTGE FLSFVIKLGF GVAQTKAVMT SISGIPMGPP RLPLVGASEE FIAKAKAKLE 


SIVWPDGD 

« Hide

References

[1]"Full-length cDNAs from chicken bursal lymphocytes to facilitate gene function analysis."
Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.
Genome Biol. 6:R6.1-R6.9(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: CB.
Tissue: Bursa of Fabricius.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ720150 mRNA. Translation: CAG31809.1.
RefSeqNP_001026731.1. NM_001031560.2.
UniGeneGga.22620.

3D structure databases

ProteinModelPortalQ5ZKD4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000038643.

Proteomic databases

PaxDbQ5ZKD4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID429074.
KEGGgga:429074.

Organism-specific databases

CTD80896.

Phylogenomic databases

eggNOGCOG0329.
HOGENOMHOG000218206.
HOVERGENHBG082055.
KOK01639.
PhylomeDBQ5ZKD4.

Enzyme and pathway databases

UniPathwayUPA00629.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR002220. DapA-like.
[Graphical view]
PANTHERPTHR12128. PTHR12128. 1 hit.
PfamPF00701. DHDPS. 1 hit.
[Graphical view]
PIRSFPIRSF001365. DHDPS. 1 hit.
PRINTSPR00146. DHPICSNTHASE.
ProtoNetSearch...

Other

NextBio20829905.
PROQ5ZKD4.

Entry information

Entry nameNPL_CHICK
AccessionPrimary (citable) accession number: Q5ZKD4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: November 23, 2004
Last modified: April 16, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways