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Protein

N-acetylneuraminate lyase

Gene

nanA

Organism
Staphylococcus aureus (strain Newman)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine (ManNAc) via a Schiff base intermediate.UniRule annotation

Catalytic activityi

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

Pathwayi: N-acetylneuraminate degradation

This protein is involved in step 1 of the subpathway that synthesizes D-fructose 6-phosphate from N-acetylneuraminate.UniRule annotation
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. N-acetylneuraminate lyase (nanA)
  2. no protein annotated in this organism
  3. Putative N-acetylmannosamine-6-phosphate 2-epimerase (nanE)
  4. no protein annotated in this organism
  5. Glucosamine-6-phosphate deaminase (nagB)
This subpathway is part of the pathway N-acetylneuraminate degradation, which is itself part of Amino-sugar metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-fructose 6-phosphate from N-acetylneuraminate, the pathway N-acetylneuraminate degradation and in Amino-sugar metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei137 – 1371Involved in proton transfer during cleavageUniRule annotation
Active sitei165 – 1651Schiff-base intermediate with substrateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

BioCyciSAUR426430:GIXC-259-MONOMER.
UniPathwayiUPA00629; UER00680.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetylneuraminate lyaseUniRule annotation (EC:4.1.3.3UniRule annotation)
Short name:
NALUniRule annotation
Short name:
Neu5Ac lyaseUniRule annotation
Alternative name(s):
N-acetylneuraminate pyruvate-lyaseUniRule annotation
N-acetylneuraminic acid aldolaseUniRule annotation
Sialate lyaseUniRule annotation
Sialic acid aldolaseUniRule annotation
Sialic acid lyaseUniRule annotation
Gene namesi
Name:nanAUniRule annotation
Ordered Locus Names:NWMN_0257
OrganismiStaphylococcus aureus (strain Newman)
Taxonomic identifieri426430 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000006386 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 293293N-acetylneuraminate lyasePRO_1000073171Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA6QDU7.
SMRiA6QDU7. Positions 2-293.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 492Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the DapA family. NanA subfamily.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000173608.
KOiK01639.
OMAiTGEFNML.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01237. N_acetylneuram_lyase. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR002220. DapA-like.
IPR005264. NanA.
IPR020625. Schiff_base-form_aldolases_AS.
[Graphical view]
PANTHERiPTHR12128. PTHR12128. 1 hit.
PfamiPF00701. DHDPS. 1 hit.
[Graphical view]
PIRSFiPIRSF001365. DHDPS. 1 hit.
PRINTSiPR00146. DHPICSNTHASE.
SMARTiSM01130. DHDPS. 1 hit.
[Graphical view]
PROSITEiPS00666. DHDPS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A6QDU7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKDLKGLYA ALLVPFDENG QVNEQGLKQI AQNAIETEEL DGLYVNGSSG
60 70 80 90 100
ENFLLNTEQK KQVFKVAKEA VGDKVKLIAQ VGSLDLNEAI ELGKYATELG
110 120 130 140 150
YDALSAVTPF YYPFTFEEIR DYYFDIIEAT QNNMIIYAIP DLTGVNISIE
160 170 180 190 200
QFSELFNHEK IVGVKYTAPN FFLLERIRKA FPDKLILSGF DEMLVQATIS
210 220 230 240 250
GVDGAIGSTY NVNGRRARKI FDLARQGQIQ EAYQLQHDSN DIIETVLSMG
260 270 280 290
IYPTLKEILR HRGIDAGLPK RPFKPFNEAH RQTLDQLIAK YDL
Length:293
Mass (Da):33,043
Last modified:August 21, 2007 - v1
Checksum:i62D7DEFFDC1AF431
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009351 Genomic DNA. Translation: BAF66529.1.
RefSeqiWP_001030738.1. NC_009641.1.

Genome annotation databases

EnsemblBacteriaiBAF66529; BAF66529; NWMN_0257.
KEGGisae:NWMN_0257.
PATRICi19583864. VBIStaAur133992_0275.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009351 Genomic DNA. Translation: BAF66529.1.
RefSeqiWP_001030738.1. NC_009641.1.

3D structure databases

ProteinModelPortaliA6QDU7.
SMRiA6QDU7. Positions 2-293.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAF66529; BAF66529; NWMN_0257.
KEGGisae:NWMN_0257.
PATRICi19583864. VBIStaAur133992_0275.

Phylogenomic databases

HOGENOMiHOG000173608.
KOiK01639.
OMAiTGEFNML.

Enzyme and pathway databases

UniPathwayiUPA00629; UER00680.
BioCyciSAUR426430:GIXC-259-MONOMER.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01237. N_acetylneuram_lyase. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR002220. DapA-like.
IPR005264. NanA.
IPR020625. Schiff_base-form_aldolases_AS.
[Graphical view]
PANTHERiPTHR12128. PTHR12128. 1 hit.
PfamiPF00701. DHDPS. 1 hit.
[Graphical view]
PIRSFiPIRSF001365. DHDPS. 1 hit.
PRINTSiPR00146. DHPICSNTHASE.
SMARTiSM01130. DHDPS. 1 hit.
[Graphical view]
PROSITEiPS00666. DHDPS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNANA_STAAE
AccessioniPrimary (citable) accession number: A6QDU7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: August 21, 2007
Last modified: September 7, 2016
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.