N-acetylneuraminate lyase - Escherichia coli (strain K12)

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P0A6L4 (NANA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 63. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
N-acetylneuraminate lyase
EC=4.1.3.3

Alternative name(s):
N-acetylneuraminate pyruvate-lyase
N-acetylneuraminic acid aldolase
NALase
Sialate lyase
Sialic acid aldolase
Sialic acid lyase

Gene names

Name:	nanA
Synonyms:	npl
Ordered Locus Names:	b3225, JW3194

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	297 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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. HAMAP MF_01237
Catalytic activity	N-acetylneuraminate = N-acetyl-D-mannosamine + pyruvate. HAMAP MF_01237
Enzyme regulation	Inhibited by reduction with NaBH₄, and by Cu²⁺ ions, p-chloromercuribenzoate and N-bromosuccinimide. HAMAP MF_01237
Pathway	Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 1/5. HAMAP MF_01237
Subunit structure	Homotetramer. Ref.6
Subcellular location	Cytoplasm HAMAP MF_01237.
Induction	By N-acetylneuraminate. HAMAP MF_01237
Sequence similarities	Belongs to the DHDPS family. NanA subfamily.
Biophysicochemical properties	pH dependence: Optimum pH is 6.5-7.0. HAMAP MF_01237 Temperature dependence: Optimum temperature is 80 degrees Celsius.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Cytoplasm
Ligand	Schiff base
Molecular function	Lyase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	N-acetylneuraminate catabolic process Inferred from mutant phenotype. Source: EcoCyc
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	N-acetylneuraminate lyase activity Inferred from direct assay Ref.5. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.5

Chain

2 – 297

296

N-acetylneuraminate lyase HAMAP MF_01237

PRO_0000103209

Regions

Region

47 – 48

Substrate binding HAMAP MF_01237

Sites

Active site

165

Schiff-base intermediate with substrate

Site

137

Involved in proton transfer during cleavage

Experimental info

Sequence conflict

A → G in CAA27051. Ref.1

Sequence conflict

S → T in CAA27051. Ref.1

Sequence conflict

282

L → Q in CAA27051. Ref.1

Secondary structure

297

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A6L4 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: BA9F30B4A7624167
Show »

FASTA

297

32,593

        10         20         30         40         50         60 
MATNLRGVMA ALLTPFDQQQ ALDKASLRRL VQFNIQQGID GLYVGGSTGE AFVQSLSERE 

        70         80         90        100        110        120 
QVLEIVAEEA KGKIKLIAHV GCVSTAESQQ LAASAKRYGF DAVSAVTPFY YPFSFEEHCD 

       130        140        150        160        170        180 
HYRAIIDSAD GLPMVVYNIP ALSGVKLTLD QINTLVTLPG VGALKQTSGD LYQMEQIRRE 

       190        200        210        220        230        240 
HPDLVLYNGY DEIFASGLLA GADGGIGSTY NIMGWRYQGI VKALKEGDIQ TAQKLQTECN 

       250        260        270        280        290 
KVIDLLIKTG VFRGLKTVLH YMDVVSVPLC RKPFGPVDEK YLPELKALAQ QLMQERG

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete nucleotide sequence of the E. coli N-acetylneuraminate lyase." Ohta Y., Watanabe K., Kimura A. Nucleic Acids Res. 13:8843-8852(1985) [PubMed: 3909108] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: K12.
[2]	"Nucleotide sequence of the N-acetylneuraminate lyase gene of Escherichia coli." Kawakami B., Kudo T., Narahashi Y., Horikoshi K. Agric. Biol. Chem. 50:2155-2158(1986) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: JE1011.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Purification, crystallization and characterization of N-acetylneuraminate lyase from Escherichia coli." Aisaka K., Igarashi A., Yamaguchi K., Uwajima T. Biochem. J. 276:541-546(1991) [PubMed: 1646603] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-24, CHARACTERIZATION. Strain: K12 / C600 / SF8.
[6]	"The three-dimensional structure of N-acetylneuraminate lyase from Escherichia coli." Izard T., Lawrence M.C., Malby R.L., Lilley G.G., Colman P.M. Structure 2:361-369(1994) [PubMed: 8081752] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SUBUNIT.
[7]	"Structure and mechanism of a sub-family of enzymes related to N-acetylneuraminate lyase." Lawrence M.C., Barbosa J.A.R.G., Smith B.J., Hall N.E., Pilling P.A., Ooi H.C., Marcuccio S.M. J. Mol. Biol. 266:381-399(1997) [PubMed: 9047371] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF COMPLEXES WITH HYDROXYPYRUVATE AND PYRUVATE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

WZECN. JP0002.

RefSeq

NP_417692.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FDY	X-ray	2.45	A/B/C/D	1-297	[»]
1FDZ	X-ray	2.60	A/B/C/D	1-297	[»]
1HL2	X-ray	1.80	A/B/C/D	1-297	[»]
1NAL	X-ray	2.20	1/2/3/4	4-297	[»]
2WKJ	X-ray	1.45	A/B/C/D	2-296	[»]
2WNN	X-ray	1.65	A/B/C/D	2-296	[»]
2WNQ	X-ray	1.80	A/B/C/D	2-297	[»]
2WNZ	X-ray	1.85	A/B/C/D	2-297	[»]
2WO5	X-ray	2.20	A/B/C/D	2-297	[»]
2WPB	X-ray	2.05	A/B/C/D	2-297	[»]
2XFW	X-ray	1.65	A/B/C/D	2-297	[»]
3LBC	X-ray	1.85	A/B/C/D	1-297	[»]
3LBM	X-ray	1.48	A/B/C/D	1-297	[»]
3LCF	X-ray	1.86	A/B/C/D	1-297	[»]
3LCG	X-ray	1.78	A/B/C/D	1-297	[»]
3LCH	X-ray	2.04	A/B/C/D	1-297	[»]
3LCI	X-ray	2.12	A/B/C/D	1-297	[»]
3LCL	X-ray	1.83	A/B/C/D	1-297	[»]
3LCW	X-ray	2.35	A/B/C/D	1-297	[»]
3LCX	X-ray	1.98	A/B/C/D	1-297	[»]

ProteinModelPortal

P0A6L4.

SMR

P0A6L4. Positions 2-296.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A6L4. 5 interactions.

2D gel databases

ECO2DBASE

G032.6. 6TH EDITION.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000000456; EBESCP00000000456; EBESCG00000000378.
EBESCT00000017947; EBESCP00000017238; EBESCG00000017003.

GeneID

947742.

GenomeReviews

Gene locus JW3194 in contig AP009048_GR.
Gene locus b3225 in contig U00096_GR.

KEGG

ecj:JW3194.
eco:b3225.

PATRIC

32121874. VBIEscCol129921_3321.

Organism-specific databases

EchoBASE

EB0631.

EcoGene

EG10637. nanA.

Phylogenomic databases

eggNOG

COG0329.

GeneTree

EBGT00050000008975.

HOGENOM

HBG358848.

OMA

DHVIIHV.

PhylomeDB

P0A6L4.

ProtClustDB

PRK04147.

Enzyme and pathway databases

BioCyc

EcoCyc:ACNEULY-MONOMER.
MetaCyc:ACNEULY-MONOMER.

Gene expression databases

Genevestigator

P0A6L4.

Family and domain databases

HAMAP

MF_01237. N-acetylneuram_lyase.
[Tree]

InterPro

IPR013785. Aldolase_TIM.
IPR002220. Dihydrodipicolinate_synth-like.
IPR020625. Dihydrodipicolinate_synth_AS.
IPR020624. Dihydrodipicolinate_synth_CS.
IPR005264. NanA.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

K01639.

PANTHER

PTHR12128. DHDPS. 1 hit.

Pfam

PF00701. DHDPS. 1 hit.
[Graphical view]

PIRSF

PIRSF001365. DHDPS. 1 hit.

PRINTS

PR00146. DHPICSNTHASE.

TIGRFAMs

TIGR00683. NanA. 1 hit.

PROSITE

PS00665. DHDPS_1. 1 hit.
PS00666. DHDPS_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

NANA_ECOLI

Accession

Primary (citable) accession number: P0A6L4
Secondary accession number(s): P06995, Q2M8Y8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 63 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents