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Protein

Spermidine N(1)-acetyltransferase

Gene

speG

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the protection against polyamine toxicity by regulating their concentration. Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to the primary amino groups of spermidine to yield N(1)- and N(8)-acetylspermidine. It can use polyamines such as spermine and N(1)-acetylspermine, but not putrescine or cadaverine.2 Publications

Catalytic activityi

Acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine.1 Publication

Enzyme regulationi

Allosterically regulated.1 Publication

Kineticsi

Kcat is 16.8 sec(-1) for acetyltransferase activity with AcCoA as substrate (in the presence of 500 µM spermine at pH 9 and 37 degrees Celsius). Kcat is 6.79 sec(-1) for acetyltransferase activity with spermine as substrate (in the presence of 100 µM AcCoA at pH 9 and 37 degrees Celsius). Kcat is 6.58 sec(-1) for acetyltransferase activity with spermidine as substrate (in the presence of 100 µM AcCoA at pH 9 and 37 degrees Celsius).1 Publication

  1. KM=99 µM for spermine (in the presence of 100 µM AcCoA at pH 9 and 37 degrees Celsius).1 Publication
  2. KM=554 µM for spermidine (in the presence of 100 µM AcCoA at pH 9 and 37 degrees Celsius).1 Publication
  3. KM=1210 µM for AcCoA (in the presence of 3 mM spermine at pH 9 and 37 degrees Celsius).1 Publication
  1. Vmax=48.1 µmol/min/mg enzyme with AcCoA as substrate (in the presence of 500 µM spermine at pH 9 and 37 degrees Celsius).1 Publication
  2. Vmax=19.4 µmol/min/mg enzyme with spermine as substrate (in the presence of 100 µM AcCoA at pH 9 and 37 degrees Celsius).1 Publication
  3. Vmax=18.8 µmol/min/mg enzyme with spermidine as substrate (in the presence of 100 µM AcCoA at pH 9 and 37 degrees Celsius).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi33 – 331Magnesium1 Publication
Binding sitei41 – 411Substrate1 Publication
Metal bindingi75 – 751Magnesium1 Publication
Sitei84 – 841Could be important for selectivity toward long polyamines1 Publication

GO - Molecular functioni

  • diamine N-acetyltransferase activity Source: UniProtKB
  • magnesium ion binding Source: UniProtKB

GO - Biological processi

  • polyamine catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Ligandi

Calcium, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciVCHO:VCA0947-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Spermidine N(1)-acetyltransferase1 Publication (EC:2.3.1.571 Publication)
Short name:
SAT1 Publication
Alternative name(s):
Spermidine/spermine N(1)-acetyltransferase1 Publication
Short name:
SSAT1 Publication
Gene namesi
Name:speG
Ordered Locus Names:VC_A0947
OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Taxonomic identifieri243277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
ProteomesiUP000000584 Componenti: Chromosome 2

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 173173Spermidine N(1)-acetyltransferasePRO_0000433302Add
BLAST

Interactioni

Subunit structurei

Homododecamer; dimer of hexamers.1 Publication

Protein-protein interaction databases

STRINGi243277.VCA0947.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EG7X-ray2.38A/B/C/D/E/F1-173[»]
4JJXX-ray2.83A/B/C1-173[»]
4JLYX-ray2.88A/B/C/D/E/F1-173[»]
4MHDX-ray2.32A/B/C1-173[»]
4MI4X-ray1.85A/B/C1-173[»]
4MJ8X-ray2.04A/B/C1-173[»]
4NCZX-ray1.89A/B/C1-173[»]
4R57X-ray2.08A/B/C/D/E/F/G/H/I/J/K/L1-173[»]
4R87X-ray2.61A/B/C/D/E/F/G/H/I/J/K/L1-173[»]
ProteinModelPortaliQ9KL03.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9KL03.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 162158N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni84 – 863Substrate binding1 Publication

Sequence similaritiesi

Belongs to the acetyltransferase family.Curated
Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

KOiK00657.
OMAiTEIQIII.
OrthoDBiEOG6D5G79.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF13302. Acetyltransf_3. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9KL03-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSQLTLRAL ERGDLRFIHN LNNNRNIMSY WFEEPYESFD ELEELYNKHI
60 70 80 90 100
HDNAERRFVV EDAQKNLIGL VELIEINYIH RSAEFQIIIA PEHQGKGFAR
110 120 130 140 150
TLINRALDYS FTILNLHKIY LHVAVENPKA VHLYEECGFV EEGHLVEEFF
160 170
INGRYQDVKR MYILQSKYLN RSE
Length:173
Mass (Da):20,675
Last modified:October 1, 2000 - v1
Checksum:i9821218EFF8E8AD8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003853 Genomic DNA. Translation: AAF96843.1.
PIRiB82398.
RefSeqiNP_233331.1. NC_002506.1.
WP_001088091.1. NC_002506.1.

Genome annotation databases

EnsemblBacteriaiAAF96843; AAF96843; VC_A0947.
GeneIDi2612395.
KEGGivch:VCA0947.
PATRICi20086424. VBIVibCho83274_3559.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003853 Genomic DNA. Translation: AAF96843.1.
PIRiB82398.
RefSeqiNP_233331.1. NC_002506.1.
WP_001088091.1. NC_002506.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EG7X-ray2.38A/B/C/D/E/F1-173[»]
4JJXX-ray2.83A/B/C1-173[»]
4JLYX-ray2.88A/B/C/D/E/F1-173[»]
4MHDX-ray2.32A/B/C1-173[»]
4MI4X-ray1.85A/B/C1-173[»]
4MJ8X-ray2.04A/B/C1-173[»]
4NCZX-ray1.89A/B/C1-173[»]
4R57X-ray2.08A/B/C/D/E/F/G/H/I/J/K/L1-173[»]
4R87X-ray2.61A/B/C/D/E/F/G/H/I/J/K/L1-173[»]
ProteinModelPortaliQ9KL03.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243277.VCA0947.

Protocols and materials databases

DNASUi2612395.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF96843; AAF96843; VC_A0947.
GeneIDi2612395.
KEGGivch:VCA0947.
PATRICi20086424. VBIVibCho83274_3559.

Phylogenomic databases

KOiK00657.
OMAiTEIQIII.
OrthoDBiEOG6D5G79.

Enzyme and pathway databases

BioCyciVCHO:VCA0947-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9KL03.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF13302. Acetyltransf_3. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 39315 / El Tor Inaba N16961.
  2. "Broad-substrate screen as a tool to identify substrates for bacterial Gcn5-related N-acetyltransferases with unknown substrate specificity."
    Kuhn M.L., Majorek K.A., Minor W., Anderson W.F.
    Protein Sci. 22:222-230(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBSTRATE SPECIFICITY.
  3. "A novel polyamine allosteric site of SpeG from Vibrio cholerae is revealed by its dodecameric structure."
    Filippova E.V., Kuhn M.L., Osipiuk J., Kiryukhina O., Joachimiak A., Ballicora M.A., Anderson W.F.
    J. Mol. Biol. 427:1316-1334(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH SUBSTRATES AND CALCIUM, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT, SUBSTRATE SPECIFICITY, REACTION MECHANISM.

Entry informationi

Entry nameiATDA_VIBCH
AccessioniPrimary (citable) accession number: Q9KL03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 24, 2015
Last sequence update: October 1, 2000
Last modified: July 22, 2015
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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 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.