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Protein

N-acetylneuraminate lyase

Gene

nanA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.

Catalytic activityi

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

Enzyme regulationi

Inhibited by reduction with NaBH4, and by Cu2+ ions, p-chloromercuribenzoate and N-bromosuccinimide.

pH dependencei

Optimum pH is 6.5-7.0.

Temperature dependencei

Optimum temperature is 80 degrees Celsius.

Pathwayi: N-acetylneuraminate degradation

This protein is involved in step 1 of the subpathway that synthesizes D-fructose 6-phosphate from N-acetylneuraminate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. N-acetylneuraminate lyase (nanA)
  2. N-acetylmannosamine kinase (nanK)
  3. Putative N-acetylmannosamine-6-phosphate 2-epimerase (nanE)
  4. N-acetylglucosamine-6-phosphate deacetylase (nagA)
  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)DescriptionActionsGraphical viewLength
Sitei137Involved in proton transfer during cleavage1
Active sitei165Schiff-base intermediate with substrate1

GO - Molecular functioni

  • identical protein binding Source: EcoCyc
  • N-acetylneuraminate lyase activity Source: EcoCyc

GO - Biological processi

  • carbohydrate metabolic process Source: UniProtKB-HAMAP
  • N-acetylneuraminate catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

BioCyciEcoCyc:ACNEULY-MONOMER.
ECOL316407:JW3194-MONOMER.
MetaCyc:ACNEULY-MONOMER.
BRENDAi4.1.3.3. 2026.
SABIO-RKP0A6L4.
UniPathwayiUPA00629; UER00680.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetylneuraminate lyase (EC:4.1.3.3)
Short name:
NAL
Short name:
Neu5Ac lyase
Alternative name(s):
N-acetylneuraminate pyruvate-lyase
N-acetylneuraminic acid aldolase
NALase
Sialate lyase
Sialic acid aldolase
Sialic acid lyase
Gene namesi
Name:nanA
Synonyms:npl
Ordered Locus Names:b3225, JW3194
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10637. nanA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001032092 – 297N-acetylneuraminate lyaseAdd BLAST296

Proteomic databases

PaxDbiP0A6L4.
PRIDEiP0A6L4.

Expressioni

Inductioni

By N-acetylneuraminate.

Interactioni

Subunit structurei

Homotetramer.1 Publication

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4262442. 341 interactors.
DIPiDIP-10302N.
IntActiP0A6L4. 5 interactors.
STRINGi511145.b3225.

Structurei

Secondary structure

1297
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 5Combined sources4
Beta strandi7 – 11Combined sources5
Beta strandi20 – 22Combined sources3
Helixi24 – 36Combined sources13
Beta strandi40 – 46Combined sources7
Turni47 – 50Combined sources4
Helixi51 – 53Combined sources3
Helixi56 – 70Combined sources15
Turni71 – 73Combined sources3
Beta strandi74 – 79Combined sources6
Helixi85 – 98Combined sources14
Beta strandi101 – 106Combined sources6
Helixi115 – 129Combined sources15
Beta strandi134 – 138Combined sources5
Helixi140 – 143Combined sources4
Helixi149 – 156Combined sources8
Beta strandi161 – 166Combined sources6
Helixi171 – 180Combined sources10
Beta strandi185 – 188Combined sources4
Helixi191 – 193Combined sources3
Helixi194 – 200Combined sources7
Beta strandi204 – 207Combined sources4
Helixi210 – 226Combined sources17
Helixi229 – 249Combined sources21
Helixi251 – 261Combined sources11
Beta strandi265 – 267Combined sources3
Helixi279 – 281Combined sources3
Helixi282 – 295Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FDYX-ray2.45A/B/C/D1-297[»]
1FDZX-ray2.60A/B/C/D1-297[»]
1HL2X-ray1.80A/B/C/D1-297[»]
1NALX-ray2.201/2/3/41-297[»]
2WKJX-ray1.45A/B/C/D2-296[»]
2WNNX-ray1.65A/B/C/D2-296[»]
2WNQX-ray1.80A/B/C/D2-297[»]
2WNZX-ray1.85A/B/C/D2-297[»]
2WO5X-ray2.20A/B/C/D2-297[»]
2WPBX-ray2.05A/B/C/D2-297[»]
2XFWX-ray1.65A/B/C/D2-297[»]
2YGYX-ray1.90A/B/C/D2-297[»]
3LBCX-ray1.85A/B/C/D1-297[»]
3LBMX-ray1.48A/B/C/D1-297[»]
3LCFX-ray1.86A/B/C/D1-297[»]
3LCGX-ray1.78A/B/C/D1-297[»]
3LCHX-ray2.04A/B/C/D1-297[»]
3LCIX-ray2.12A/B/C/D1-297[»]
3LCLX-ray1.83A/B/C/D1-297[»]
3LCWX-ray2.35A/B/C/D1-297[»]
3LCXX-ray1.98A/B/C/D1-297[»]
4BWLX-ray2.00A/B/C/D2-297[»]
4UUIX-ray1.79A/B/C/D2-297[»]
ProteinModelPortaliP0A6L4.
SMRiP0A6L4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6L4.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni47 – 48Substrate binding2

Sequence similaritiesi

Belongs to the DapA family. NanA subfamily.Curated

Phylogenomic databases

eggNOGiENOG4105CDP. Bacteria.
COG0329. LUCA.
HOGENOMiHOG000173608.
InParanoidiP0A6L4.
KOiK01639.
OMAiDVPWLAQ.
PhylomeDBiP0A6L4.

Family and domain databases

CDDicd00954. NAL. 1 hit.
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.
IPR020624. Schiff_base-form_aldolases_CS.
[Graphical view]
PANTHERiPTHR12128. PTHR12128. 1 hit.
PfamiPF00701. DHDPS. 1 hit.
[Graphical view]
PIRSFiPIRSF001365. DHDPS. 1 hit.
PRINTSiPR00146. DHPICSNTHASE.
SMARTiSM01130. DHDPS. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00683. nanA. 1 hit.
PROSITEiPS00665. DHDPS_1. 1 hit.
PS00666. DHDPS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A6L4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATNLRGVMA ALLTPFDQQQ ALDKASLRRL VQFNIQQGID GLYVGGSTGE
60 70 80 90 100
AFVQSLSERE QVLEIVAEEA KGKIKLIAHV GCVSTAESQQ LAASAKRYGF
110 120 130 140 150
DAVSAVTPFY YPFSFEEHCD HYRAIIDSAD GLPMVVYNIP ALSGVKLTLD
160 170 180 190 200
QINTLVTLPG VGALKQTSGD LYQMEQIRRE HPDLVLYNGY DEIFASGLLA
210 220 230 240 250
GADGGIGSTY NIMGWRYQGI VKALKEGDIQ TAQKLQTECN KVIDLLIKTG
260 270 280 290
VFRGLKTVLH YMDVVSVPLC RKPFGPVDEK YLPELKALAQ QLMQERG
Length:297
Mass (Da):32,593
Last modified:January 23, 2007 - v2
Checksum:iBA9F30B4A7624167
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti70A → G in CAA27051 (PubMed:3909108).Curated1
Sequence conflicti84S → T in CAA27051 (PubMed:3909108).Curated1
Sequence conflicti282L → Q in CAA27051 (PubMed:3909108).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03345 Genomic DNA. Translation: CAA27051.1.
D00067 Genomic DNA. Translation: BAA00046.1.
U18997 Genomic DNA. Translation: AAA58027.1.
U00096 Genomic DNA. Translation: AAC76257.1.
AP009048 Genomic DNA. Translation: BAE77268.1.
PIRiJP0002. WZECN.
RefSeqiNP_417692.1. NC_000913.3.
WP_000224714.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76257; AAC76257; b3225.
BAE77268; BAE77268; BAE77268.
GeneIDi947742.
KEGGiecj:JW3194.
eco:b3225.
PATRICi32121874. VBIEscCol129921_3321.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03345 Genomic DNA. Translation: CAA27051.1.
D00067 Genomic DNA. Translation: BAA00046.1.
U18997 Genomic DNA. Translation: AAA58027.1.
U00096 Genomic DNA. Translation: AAC76257.1.
AP009048 Genomic DNA. Translation: BAE77268.1.
PIRiJP0002. WZECN.
RefSeqiNP_417692.1. NC_000913.3.
WP_000224714.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FDYX-ray2.45A/B/C/D1-297[»]
1FDZX-ray2.60A/B/C/D1-297[»]
1HL2X-ray1.80A/B/C/D1-297[»]
1NALX-ray2.201/2/3/41-297[»]
2WKJX-ray1.45A/B/C/D2-296[»]
2WNNX-ray1.65A/B/C/D2-296[»]
2WNQX-ray1.80A/B/C/D2-297[»]
2WNZX-ray1.85A/B/C/D2-297[»]
2WO5X-ray2.20A/B/C/D2-297[»]
2WPBX-ray2.05A/B/C/D2-297[»]
2XFWX-ray1.65A/B/C/D2-297[»]
2YGYX-ray1.90A/B/C/D2-297[»]
3LBCX-ray1.85A/B/C/D1-297[»]
3LBMX-ray1.48A/B/C/D1-297[»]
3LCFX-ray1.86A/B/C/D1-297[»]
3LCGX-ray1.78A/B/C/D1-297[»]
3LCHX-ray2.04A/B/C/D1-297[»]
3LCIX-ray2.12A/B/C/D1-297[»]
3LCLX-ray1.83A/B/C/D1-297[»]
3LCWX-ray2.35A/B/C/D1-297[»]
3LCXX-ray1.98A/B/C/D1-297[»]
4BWLX-ray2.00A/B/C/D2-297[»]
4UUIX-ray1.79A/B/C/D2-297[»]
ProteinModelPortaliP0A6L4.
SMRiP0A6L4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262442. 341 interactors.
DIPiDIP-10302N.
IntActiP0A6L4. 5 interactors.
STRINGi511145.b3225.

Proteomic databases

PaxDbiP0A6L4.
PRIDEiP0A6L4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76257; AAC76257; b3225.
BAE77268; BAE77268; BAE77268.
GeneIDi947742.
KEGGiecj:JW3194.
eco:b3225.
PATRICi32121874. VBIEscCol129921_3321.

Organism-specific databases

EchoBASEiEB0631.
EcoGeneiEG10637. nanA.

Phylogenomic databases

eggNOGiENOG4105CDP. Bacteria.
COG0329. LUCA.
HOGENOMiHOG000173608.
InParanoidiP0A6L4.
KOiK01639.
OMAiDVPWLAQ.
PhylomeDBiP0A6L4.

Enzyme and pathway databases

UniPathwayiUPA00629; UER00680.
BioCyciEcoCyc:ACNEULY-MONOMER.
ECOL316407:JW3194-MONOMER.
MetaCyc:ACNEULY-MONOMER.
BRENDAi4.1.3.3. 2026.
SABIO-RKP0A6L4.

Miscellaneous databases

EvolutionaryTraceiP0A6L4.
PROiP0A6L4.

Family and domain databases

CDDicd00954. NAL. 1 hit.
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.
IPR020624. Schiff_base-form_aldolases_CS.
[Graphical view]
PANTHERiPTHR12128. PTHR12128. 1 hit.
PfamiPF00701. DHDPS. 1 hit.
[Graphical view]
PIRSFiPIRSF001365. DHDPS. 1 hit.
PRINTSiPR00146. DHPICSNTHASE.
SMARTiSM01130. DHDPS. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00683. nanA. 1 hit.
PROSITEiPS00665. DHDPS_1. 1 hit.
PS00666. DHDPS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNANA_ECOLI
AccessioniPrimary (citable) accession number: P0A6L4
Secondary accession number(s): P06995, Q2M8Y8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.