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Q29RY9 (NPL_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. 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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

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_0000273351

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
Q29RY9 [UniParc].

Last modified April 4, 2006. Version 1.
Checksum: D91F221361E56BA6

FASTA32035,166
        10         20         30         40         50         60 
MASPKKKLQG LVAATITPMT EHGEINFSVI GRYVDYLVEE QGVKNVFVNG TTGEGLSLSI 

        70         80         90        100        110        120 
SERCQVAEEW VTKGKNKLDQ IVIHVGALSL KESQELAQHA AEIGADGIAV IAPFFLKPWN 

       130        140        150        160        170        180 
KDVLINFLKE VAAAAPALPF YYYHIPALTG VKIRAEELLD GIQDKIPSFQ GLKFSDTDLL 

       190        200        210        220        230        240 
DFGQCVDQNR QRQFAFLFGV DEQLLSALVM GATGAVGSTY NYLGKKTKQM LEAFERKDFS 

       250        260        270        280        290        300 
SALNHQFCIQ RFINFVVKLG FGVSQTKAIM TLVSGIPMGP PRLPLQKASR EFTDNAEAKL 

       310        320 
KSLDFLSCTD LKDGNMEACS 

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Uterus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC113332 mRNA. Translation: AAI13333.1.
RefSeqNP_001039443.1. NM_001045978.1.
XP_005217334.1. XM_005217277.1.
XP_005217335.1. XM_005217278.1.
UniGeneBt.26155.

3D structure databases

ProteinModelPortalQ29RY9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000002925.

Proteomic databases

PRIDEQ29RY9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000002925; ENSBTAP00000002925; ENSBTAG00000002266.
GeneID507597.
KEGGbta:507597.

Organism-specific databases

CTD80896.

Phylogenomic databases

eggNOGCOG0329.
GeneTreeENSGT00530000063604.
HOGENOMHOG000218206.
HOVERGENHBG082055.
InParanoidQ29RY9.
KOK01639.
OMAPWNKDVL.
OrthoDBEOG7NKKKP.
TreeFamTF353639.

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

NextBio20868136.

Entry information

Entry nameNPL_BOVIN
AccessionPrimary (citable) accession number: Q29RY9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: April 4, 2006
Last modified: February 19, 2014
This is version 64 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