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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

Manual assertion based on experiment ini

  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)DescriptionActionsGraphical viewLength
Metal bindingi33Magnesium1 Publication1
Binding sitei41Substrate1 Publication1
Metal bindingi75Magnesium1 Publication1
Sitei84Could be important for selectivity toward long polyamines1 Publication1

GO - Molecular functioni

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

GO - Biological processi

  • N-terminal protein amino acid acetylation Source: GO_Central
  • 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
Proteomesi
  • UP000000584 Componenti: Chromosome 2

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004333021 – 173Spermidine N(1)-acetyltransferaseAdd BLAST173

Interactioni

Subunit structurei

Homododecamer; dimer of hexamers.1 Publication

Protein-protein interaction databases

STRINGi243277.VCA0947.

Structurei

Secondary structure

1173
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 4Combined sources3
Beta strandi6 – 9Combined sources4
Helixi12 – 14Combined sources3
Helixi15 – 22Combined sources8
Helixi25 – 28Combined sources4
Helixi29 – 31Combined sources3
Beta strandi34 – 36Combined sources3
Helixi39 – 48Combined sources10
Turni49 – 51Combined sources3
Beta strandi56 – 61Combined sources6
Beta strandi67 – 77Combined sources11
Turni78 – 81Combined sources4
Beta strandi82 – 89Combined sources8
Helixi91 – 93Combined sources3
Beta strandi95 – 97Combined sources3
Helixi99 – 112Combined sources14
Beta strandi117 – 124Combined sources8
Helixi128 – 136Combined sources9
Beta strandi140 – 151Combined sources12
Beta strandi154 – 164Combined sources11
Helixi165 – 169Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
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[»]
4YGOX-ray2.50A/B/C/D/E/F1-173[»]
5CNPX-ray2.38A/B/C/D/E/F1-173[»]
ProteinModelPortaliQ9KL03.
SMRiQ9KL03.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9KL03.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 162N-acetyltransferasePROSITE-ProRule annotationAdd BLAST158

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni84 – 86Substrate binding1 Publication3

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108HK0. Bacteria.
ENOG411253A. LUCA.
KOiK00657.
OMAiYRDVKRM.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
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[»]
4YGOX-ray2.50A/B/C/D/E/F1-173[»]
5CNPX-ray2.38A/B/C/D/E/F1-173[»]
ProteinModelPortaliQ9KL03.
SMRiQ9KL03.
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

eggNOGiENOG4108HK0. Bacteria.
ENOG411253A. LUCA.
KOiK00657.
OMAiYRDVKRM.

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...

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: November 2, 2016
This is version 84 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

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.