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Q2G160

- NANA_STAA8

UniProt

Q2G160 - NANA_STAA8

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Protein

N-acetylneuraminate lyase

Gene

nanA

Organism
Staphylococcus aureus (strain NCTC 8325)
Status
Reviewed - 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.1 PublicationUniRule annotation

Catalytic activityi

N-acetylneuraminate = N-acetyl-D-mannosamine + pyruvate.1 PublicationUniRule annotation

Kineticsi

kcat is 250 min(-1) for the cleavage of Neu5Ac at pH 7.4, and is 260 min(-1) at pH 6.8.1 Publication

  1. KM=2.2 mM for N-acetylneuraminate (at pH 7.4)1 Publication
  2. KM=2.4 mM for N-acetylneuraminate (at pH 6.8)1 Publication

pH dependencei

Optimum pH is 7.4.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei137 – 1371Involved in proton transfer during cleavageUniRule annotation
Active sitei165 – 1651Schiff-base intermediate with substrate1 PublicationUniRule annotation

GO - Molecular functioni

  1. N-acetylneuraminate lyase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. carbohydrate metabolic process Source: UniProtKB-HAMAP
  2. N-acetylneuraminate catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

BioCyciSAUR93061:GIWJ-279-MONOMER.
UniPathwayiUPA00629; UER00680.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetylneuraminate lyase1 PublicationUniRule annotation (EC:4.1.3.31 PublicationUniRule annotation)
Short name:
NAL1 PublicationUniRule annotation
Short name:
Neu5Ac lyase1 PublicationUniRule 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:nanA1 PublicationUniRule annotation
Ordered Locus Names:SAOUHSC_00295
OrganismiStaphylococcus aureus (strain NCTC 8325)
Taxonomic identifieri93061 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000008816: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi165 – 1651K → C: 3125-fold decrease in catalytic activity, and 3-fold increase in substrate affinity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 293293N-acetylneuraminate lyasePRO_1000066938Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 PublicationUniRule annotation

Protein-protein interaction databases

STRINGi93061.SAOUHSC_00295.

Structurei

Secondary structure

1
293
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 115
Helixi24 – 3613
Beta strandi41 – 477
Helixi48 – 503
Helixi52 – 543
Helixi57 – 6913
Beta strandi75 – 806
Helixi86 – 9914
Beta strandi102 – 1076
Helixi116 – 13015
Beta strandi134 – 1385
Helixi140 – 1434
Helixi149 – 1568
Beta strandi161 – 1666
Helixi171 – 18010
Beta strandi184 – 1885
Helixi191 – 1933
Helixi194 – 1996
Beta strandi203 – 2086
Helixi210 – 22516
Helixi229 – 24921
Helixi251 – 26010
Turni261 – 2633
Helixi278 – 2803
Helixi281 – 29111

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AH7X-ray2.30A/B/C/D2-293[»]
4AHOX-ray2.00A/B/C/D1-293[»]
4AHPX-ray2.10A/B/C/D2-293[»]
4AHQX-ray1.95A/B/C/D2-293[»]
4AMAX-ray2.35A/B/C/D2-293[»]
ProteinModelPortaliQ2G160.
SMRiQ2G160. Positions 2-293.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 492Substrate binding1 PublicationUniRule annotation

Sequence similaritiesi

Belongs to the DapA family. NanA subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0329.
HOGENOMiHOG000173608.
KOiK01639.
OMAiELVPSDM.
OrthoDBiEOG6W7235.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q2G160-1 [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:March 21, 2006 - v1
Checksum:i62D7DEFFDC1AF431
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000253 Genomic DNA. Translation: ABD29464.1.
RefSeqiYP_498885.1. NC_007795.1.

Genome annotation databases

EnsemblBacteriaiABD29464; ABD29464; SAOUHSC_00295.
GeneIDi3918976.
KEGGisao:SAOUHSC_00295.
PATRICi19578184. VBIStaAur99865_0268.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000253 Genomic DNA. Translation: ABD29464.1 .
RefSeqi YP_498885.1. NC_007795.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4AH7 X-ray 2.30 A/B/C/D 2-293 [» ]
4AHO X-ray 2.00 A/B/C/D 1-293 [» ]
4AHP X-ray 2.10 A/B/C/D 2-293 [» ]
4AHQ X-ray 1.95 A/B/C/D 2-293 [» ]
4AMA X-ray 2.35 A/B/C/D 2-293 [» ]
ProteinModelPortali Q2G160.
SMRi Q2G160. Positions 2-293.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 93061.SAOUHSC_00295.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABD29464 ; ABD29464 ; SAOUHSC_00295 .
GeneIDi 3918976.
KEGGi sao:SAOUHSC_00295.
PATRICi 19578184. VBIStaAur99865_0268.

Phylogenomic databases

eggNOGi COG0329.
HOGENOMi HOG000173608.
KOi K01639.
OMAi ELVPSDM.
OrthoDBi EOG6W7235.

Enzyme and pathway databases

UniPathwayi UPA00629 ; UER00680 .
BioCyci SAUR93061:GIWJ-279-MONOMER.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_01237. N_acetylneuram_lyase.
InterProi IPR013785. Aldolase_TIM.
IPR002220. DapA-like.
IPR020625. Dihydrodipicolinate_synth_AS.
IPR005264. NanA.
[Graphical view ]
PANTHERi PTHR12128. PTHR12128. 1 hit.
Pfami PF00701. DHDPS. 1 hit.
[Graphical view ]
PIRSFi PIRSF001365. DHDPS. 1 hit.
PRINTSi PR00146. DHPICSNTHASE.
PROSITEi PS00666. DHDPS_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The Staphylococcus aureus NCTC 8325 genome."
    Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.
    (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.); Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington D.C. (2006)
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NCTC 8325.
  2. "Structural insights into the recovery of aldolase activity in N-acetylneuraminic acid lyase by replacement of the catalytically active lysine with gamma-thialysine by using a chemical mutagenesis strategy."
    Timms N., Windle C.L., Polyakova A., Ault J.R., Trinh C.H., Pearson A.R., Nelson A., Berry A.
    ChemBioChem 14:474-481(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF APOENZYME, WILD-TYPE AND MUTANTS CYS-165 AND GAMMA-THIALYSINE-165 IN COMPLEX WITH PYRUVATE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-165, ACTIVE SITE.
    Strain: NCTC 8325.

Entry informationi

Entry nameiNANA_STAA8
AccessioniPrimary (citable) accession number: Q2G160
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: March 21, 2006
Last modified: October 29, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

When the catalytic Lys-165 residue is replaced by the unnatural amino acid gamma-thialysine, the enzyme regains significant activity compared with the Cys-165 mutant; regains of approximately 17% of the wild-type catalytic efficiency.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3