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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)LengthDescriptionGraphical viewFeature identifierActions
Sitei137 – 1371Involved in proton transfer during cleavage
Active sitei165 – 1651Schiff-base intermediate with substrate

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 297296N-acetylneuraminate lyasePRO_0000103209Add
BLAST

Proteomic databases

PaxDbiP0A6L4.

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 interactions.
DIPiDIP-10302N.
IntActiP0A6L4. 5 interactions.
STRINGi511145.b3225.

Structurei

Secondary structure

1
297
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 54Combined sources
Beta strandi7 – 115Combined sources
Beta strandi20 – 223Combined sources
Helixi24 – 3613Combined sources
Beta strandi40 – 467Combined sources
Turni47 – 504Combined sources
Helixi51 – 533Combined sources
Helixi56 – 7015Combined sources
Turni71 – 733Combined sources
Beta strandi74 – 796Combined sources
Helixi85 – 9814Combined sources
Beta strandi101 – 1066Combined sources
Helixi115 – 12915Combined sources
Beta strandi134 – 1385Combined sources
Helixi140 – 1434Combined sources
Helixi149 – 1568Combined sources
Beta strandi161 – 1666Combined sources
Helixi171 – 18010Combined sources
Beta strandi185 – 1884Combined sources
Helixi191 – 1933Combined sources
Helixi194 – 2007Combined sources
Beta strandi204 – 2074Combined sources
Helixi210 – 22617Combined sources
Helixi229 – 24921Combined sources
Helixi251 – 26111Combined sources
Beta strandi265 – 2673Combined sources
Helixi279 – 2813Combined sources
Helixi282 – 29514Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-296.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6L4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni47 – 482Substrate binding

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

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti70 – 701A → G in CAA27051 (PubMed:3909108).Curated
Sequence conflicti84 – 841S → T in CAA27051 (PubMed:3909108).Curated
Sequence conflicti282 – 2821L → Q in CAA27051 (PubMed:3909108).Curated

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
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. Positions 2-296.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

PaxDbiP0A6L4.

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

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: September 7, 2016
This is version 101 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.