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Q66H59 (NPL_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 80. 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length320 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 – 320320N-acetylneuraminate lyase
PRO_0000273356

Regions

Region51 – 522Substrate binding By similarity

Sites

Active site1731Schiff-base intermediate with substrate By similarity
Site1431Involved in proton transfer during cleavage By similarity

Sequences

Sequence LengthMass (Da)Tools
Q66H59 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 3674F314288D8B89

FASTA32035,115
        10         20         30         40         50         60 
MAFPKKKLQG LVAATITPMT ENGEINFPVI GQYVDYLVKE QGVKNIFVNG TTGEGLSLSI 

        70         80         90        100        110        120 
SERRQVAEEW VRQGKNKLDQ VVIHVGALNL KESQELAQHA AEIGADGIAV IAPFFFKSQN 

       130        140        150        160        170        180 
KDALISFLRE VAAAAPALPF YYYHIPSLTG VKIRAEELLD GIQDKIPSFQ GLKFSDTDLL 

       190        200        210        220        230        240 
DFGQCVDQNH QRQFALLFGV DEQLLSALVL GATGAVGSTY NYLGKKTNQM LEAFEQKDLA 

       250        260        270        280        290        300 
SALSYQFRIQ RFINYVIKLG FGVSQTKAIM TLVSGIPMGP PRLPLQKATQ EFTANAEAKL 

       310        320 
KSLNFLSFPG LKDGNMEACS 

« Hide

References

[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC082004 mRNA. Translation: AAH82004.1.
RefSeqNP_001014006.1. NM_001013984.1.
UniGeneRn.114492.

3D structure databases

ProteinModelPortalQ66H59.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000003713.

Proteomic databases

PaxDbQ66H59.
PRIDEQ66H59.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000003713; ENSRNOP00000003713; ENSRNOG00000002775.
GeneID304860.
KEGGrno:304860.
UCSCRGD:1549702. rat.

Organism-specific databases

CTD80896.
RGD1549702. Npl.

Phylogenomic databases

eggNOGCOG0329.
GeneTreeENSGT00530000063604.
HOGENOMHOG000218206.
HOVERGENHBG082055.
InParanoidQ66H59.
KOK01639.
OMAPWNKDVL.
OrthoDBEOG7NKKKP.
PhylomeDBQ66H59.
TreeFamTF353639.

Enzyme and pathway databases

UniPathwayUPA00629.

Gene expression databases

GenevestigatorQ66H59.

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

NextBio653735.
PROQ66H59.

Entry information

Entry nameNPL_RAT
AccessionPrimary (citable) accession number: Q66H59
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: October 11, 2004
Last modified: April 16, 2014
This is version 80 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