Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Polyamine aminopropyltransferase

Gene

speE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of polyamines which play a significant role in the structural and functional organization in the chromoid of E.coli by compacting DNA and neutralizing negative charges. Catalyzes the irreversible transfer (ping-pong mechanism) of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine. Cadaverine (1,5-diaminopentane) and spermidine can also be used as the propylamine acceptor.2 Publications

Catalytic activityi

S-adenosyl 3-(methylthio)propylamine + putrescine = 5'-S-methyl-5'-thioadenosine + spermidine.UniRule annotation2 Publications
S-adenosyl 3-(methylthio)propylamine + spermidine = S-methyl-5'-thioadenosine + spermine.1 Publication
S-adenosyl 3-(methylthio)propylamine + 1,5-diaminopentane = S-methyl-5'-thioadenosine + N-(3-aminopropyl)-1,5-diaminopentane.1 Publication
S-adenosyl 3-(methylthio)propylamine + spermidine = S-methyl-5'-thioadenosine + thermospermine + H+.1 Publication

Enzyme regulationi

The activity is thought to be regulated mainly by the availability of decarboxylated S-adenosylmethionine. Inhibited by dicyclohexylamine, S-adenosyl-1,8-diamino-3-thiooctane (AdoDATO), sulfonium-deaminated analogs of S-adenosyl(5')-3-methylthiopropylamine, p-hydroxymercuribenzoate and N-ethylmaleimide.4 Publications

Kineticsi

  1. KM=2.2 µM for S-adenosylmethionine1 Publication
  2. KM=12 µM for putrescine1 Publication
  3. KM=77.77 µM for putrescine (at pH 7.5 and 37 degrees Celsius)1 Publication
  4. KM=84.98 µM for S-adenosylmethionine (at pH 7.5 and 37 degrees Celsius)1 Publication
  1. Vmax=2 µmol/min/mg enzyme1 Publication
  2. Vmax=0.560 µmol/min/mg enzyme (at pH 7.5 and 37 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 7.5.1 Publication

Temperature dependencei

Optimum temperature is 50 degrees Celsius.1 Publication

Pathwayi: spermidine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes spermidine from putrescine.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Polyamine aminopropyltransferase (speE)
This subpathway is part of the pathway spermidine biosynthesis, which is itself part of Amine and polyamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes spermidine from putrescine, the pathway spermidine biosynthesis and in Amine and polyamine biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei9 – 91PolyamineUniRule annotation
Binding sitei33 – 331S-adenosylmethioninamineUniRule annotation
Binding sitei64 – 641PolyamineUniRule annotation
Binding sitei88 – 881PolyamineUniRule annotation
Binding sitei108 – 1081S-adenosylmethioninamineUniRule annotation
Active sitei158 – 1581Proton acceptor1 Publication
Binding sitei165 – 1651S-adenosylmethioninamine; via carbonyl oxygenUniRule annotation

GO - Molecular functioni

  • cadaverine aminopropyltransferase activity Source: UniProtKB
  • spermidine synthase activity Source: EcoCyc
  • spermine synthase activity Source: UniProtKB-EC
  • thermospermine synthase activity Source: UniProtKB

GO - Biological processi

  • spermidine biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Polyamine biosynthesis, Spermidine biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:SPERMIDINESYN-MONOMER.
ECOL316407:JW0117-MONOMER.
MetaCyc:SPERMIDINESYN-MONOMER.
BRENDAi2.5.1.16. 2026.
UniPathwayiUPA00248; UER00314.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyamine aminopropyltransferase1 PublicationUniRule annotation
Alternative name(s):
Cadaverine aminopropyltransferase1 Publication (EC:2.5.1.-1 Publication)
Putrescine aminopropyltransferaseUniRule annotation1 Publication
Short name:
PAPTUniRule annotation
Spermidine aminopropyltransferase1 Publication (EC:2.5.1.791 Publication)
Spermidine synthase1 PublicationUniRule annotation (EC:2.5.1.16UniRule annotation2 Publications)
Short name:
SPDS1 PublicationUniRule annotation
Short name:
SPDSY1 PublicationUniRule annotation
Spermine synthase1 Publication (EC:2.5.1.221 Publication)
Thermospermine synthase1 Publication
Gene namesi
Name:speE1 PublicationUniRule annotation
Ordered Locus Names:b0121, JW0117
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10963. speE.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi158 – 1581D → A: Completely inactive. 1 Publication
Mutagenesisi159 – 1591C → A: Reduction of 23% of the aminopropyltransferase activity. 1 Publication
Mutagenesisi159 – 1591C → S: No influence on aminopropyltransferase activity. 1 Publication
Mutagenesisi160 – 1601T → A: Reduction of aminopropyltransferase activity. 1 Publication
Mutagenesisi161 – 1611D → A: Completely inactive. 1 Publication
Mutagenesisi162 – 1621P → A: No influence on aminopropyltransferase activity. 1 Publication
Mutagenesisi163 – 1631I → A: No influence on aminopropyltransferase activity. 1 Publication
Mutagenesisi165 – 1651P → A: Reduction of aminopropyltransferase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 288287Polyamine aminopropyltransferasePRO_0000156479Add
BLAST

Proteomic databases

PaxDbiP09158.
PRIDEiP09158.

2D gel databases

SWISS-2DPAGEP09158.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi4262092. 235 interactions.
IntActiP09158. 11 interactions.
MINTiMINT-1231846.
STRINGi511145.b0121.

Structurei

Secondary structure

1
288
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84Combined sources
Beta strandi11 – 2818Combined sources
Beta strandi30 – 323Combined sources
Beta strandi35 – 406Combined sources
Turni41 – 433Combined sources
Beta strandi44 – 496Combined sources
Beta strandi52 – 565Combined sources
Turni57 – 593Combined sources
Helixi60 – 7415Combined sources
Beta strandi80 – 856Combined sources
Helixi90 – 967Combined sources
Beta strandi103 – 1097Combined sources
Helixi111 – 12010Combined sources
Helixi122 – 1254Combined sources
Helixi128 – 1303Combined sources
Beta strandi134 – 1396Combined sources
Turni141 – 1455Combined sources
Beta strandi152 – 1587Combined sources
Helixi173 – 1808Combined sources
Beta strandi182 – 19716Combined sources
Helixi200 – 21213Combined sources
Beta strandi214 – 2218Combined sources
Beta strandi226 – 2294Combined sources
Beta strandi231 – 2388Combined sources
Helixi242 – 2443Combined sources
Helixi247 – 2559Combined sources
Helixi266 – 2727Combined sources
Helixi277 – 2826Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3O4FX-ray2.90A/B/C/D/E/F/G/H1-288[»]
ProteinModelPortaliP09158.
SMRiP09158. Positions 4-287.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 238230PABSUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 542Polyamine bindingUniRule annotation
Regioni140 – 1412S-adenosylmethioninamine bindingUniRule annotation
Regioni159 – 1613Polyamine bindingUniRule annotation

Sequence similaritiesi

Belongs to the spermidine/spermine synthase family.UniRule annotation
Contains 1 PABS (polyamine biosynthesis) domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CCX. Bacteria.
COG0421. LUCA.
HOGENOMiHOG000256146.
InParanoidiP09158.
KOiK00797.
OMAiSGLWSFT.
PhylomeDBiP09158.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_00198. Spermidine_synth. 1 hit.
InterProiIPR030374. PABS.
IPR030373. PABS_CS.
IPR029063. SAM-dependent_MTases.
IPR001045. Spermi_synthase.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00417. speE. 1 hit.
PROSITEiPS01330. PABS_1. 1 hit.
PS51006. PABS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09158-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEKKQWHET LHDQFGQYFA VDNVLYHEKT DHQDLIIFEN AAFGRVMALD
60 70 80 90 100
GVVQTTERDE FIYHEMMTHV PLLAHGHAKH VLIIGGGDGA MLREVTRHKN
110 120 130 140 150
VESITMVEID AGVVSFCRQY LPNHNAGSYD DPRFKLVIDD GVNFVNQTSQ
160 170 180 190 200
TFDVIISDCT DPIGPGESLF TSAFYEGCKR CLNPGGIFVA QNGVCFLQQE
210 220 230 240 250
EAIDSHRKLS HYFSDVGFYQ AAIPTYYGGI MTFAWATDND ALRHLSTEII
260 270 280
QARFLASGLK CRYYNPAIHT AAFALPQYLQ DALASQPS
Length:288
Mass (Da):32,321
Last modified:January 23, 2007 - v2
Checksum:i31AE026FF6199E9F
GO

Mass spectrometryi

Molecular mass is 33823 Da from positions 1 - 288. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02804 Genomic DNA. Translation: AAA24643.1.
U00096 Genomic DNA. Translation: AAC73232.1.
AP009048 Genomic DNA. Translation: BAB96695.1.
PIRiA29778. SYECSD.
RefSeqiNP_414663.1. NC_000913.3.
WP_000818411.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73232; AAC73232; b0121.
BAB96695; BAB96695; BAB96695.
GeneIDi947726.
KEGGiecj:JW0117.
eco:b0121.
PATRICi32115343. VBIEscCol129921_0123.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02804 Genomic DNA. Translation: AAA24643.1.
U00096 Genomic DNA. Translation: AAC73232.1.
AP009048 Genomic DNA. Translation: BAB96695.1.
PIRiA29778. SYECSD.
RefSeqiNP_414663.1. NC_000913.3.
WP_000818411.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3O4FX-ray2.90A/B/C/D/E/F/G/H1-288[»]
ProteinModelPortaliP09158.
SMRiP09158. Positions 4-287.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262092. 235 interactions.
IntActiP09158. 11 interactions.
MINTiMINT-1231846.
STRINGi511145.b0121.

2D gel databases

SWISS-2DPAGEP09158.

Proteomic databases

PaxDbiP09158.
PRIDEiP09158.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73232; AAC73232; b0121.
BAB96695; BAB96695; BAB96695.
GeneIDi947726.
KEGGiecj:JW0117.
eco:b0121.
PATRICi32115343. VBIEscCol129921_0123.

Organism-specific databases

EchoBASEiEB0956.
EcoGeneiEG10963. speE.

Phylogenomic databases

eggNOGiENOG4105CCX. Bacteria.
COG0421. LUCA.
HOGENOMiHOG000256146.
InParanoidiP09158.
KOiK00797.
OMAiSGLWSFT.
PhylomeDBiP09158.

Enzyme and pathway databases

UniPathwayiUPA00248; UER00314.
BioCyciEcoCyc:SPERMIDINESYN-MONOMER.
ECOL316407:JW0117-MONOMER.
MetaCyc:SPERMIDINESYN-MONOMER.
BRENDAi2.5.1.16. 2026.

Miscellaneous databases

PROiP09158.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_00198. Spermidine_synth. 1 hit.
InterProiIPR030374. PABS.
IPR030373. PABS_CS.
IPR029063. SAM-dependent_MTases.
IPR001045. Spermi_synthase.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00417. speE. 1 hit.
PROSITEiPS01330. PABS_1. 1 hit.
PS51006. PABS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSPEE_ECOLI
AccessioniPrimary (citable) accession number: P09158
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 149 of the entry and version 2 of the sequence. [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

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.