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Protein

N-acetylneuraminate lyase

Gene

nanA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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-KW
  • N-acetylneuraminate catabolic process Source: EcoCyc

Keywordsi

Molecular functionLyase
Biological processCarbohydrate metabolism
LigandSchiff base

Enzyme and pathway databases

BioCyciEcoCyc:ACNEULY-MONOMER
MetaCyc:ACNEULY-MONOMER
BRENDAi4.1.3.3 2026
SABIO-RKiP0A6L4
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

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

Negatively regulated by the transcriptional repressor NanR. Induced by N-acetylneuraminate, via inactivation of NanR.1 Publication

Interactioni

Subunit structurei

Homotetramer.1 Publication

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4262442, 344 interactors
DIPiDIP-10302N
IntActiP0A6L4, 5 interactors
STRINGi316385.ECDH10B_3402

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
OMAiSALNHQF
PhylomeDBiP0A6L4

Family and domain databases

CDDicd00954 NAL, 1 hit
Gene3Di3.20.20.70, 1 hit
HAMAPiMF_01237 N_acetylneuram_lyase, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR002220 DapA-like
IPR005264 NanA
IPR020625 Schiff_base-form_aldolases_AS
IPR020624 Schiff_base-form_aldolases_CS
PANTHERiPTHR42849 PTHR42849, 1 hit
PfamiView protein in Pfam
PF00701 DHDPS, 1 hit
PIRSFiPIRSF001365 DHDPS, 1 hit
PRINTSiPR00146 DHPICSNTHASE
SMARTiView protein in SMART
SM01130 DHDPS, 1 hit
TIGRFAMsiTIGR00683 nanA, 1 hit
PROSITEiView protein in PROSITE
PS00665 DHDPS_1, 1 hit
PS00666 DHDPS_2, 1 hit

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
PATRICifig|1411691.4.peg.3503

Similar proteinsi

Entry informationi

Entry nameiNANA_ECOLI
AccessioniPrimary (citable) accession number: P0A6L4
Secondary accession number(s): P06995, Q2M8Y8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 110 of the entry and version 2 of the sequence. See 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

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