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P09158 (SPEE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Spermidine synthase

EC=2.5.1.16
Alternative name(s):
Putrescine aminopropyltransferase
Short name=PAPT
SPDSY
Gene names
Name:speE
Ordered Locus Names:b0121, JW0117
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length288 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the production of spermidine from putrescine and decarboxylated S-adenosylmethionine (dcSAM), which serves as an aminopropyl donor. HAMAP-Rule MF_00198

Catalytic activity

S-adenosylmethioninamine + putrescine = S-methyl-5'-thioadenosine + spermidine. HAMAP-Rule MF_00198

Enzyme regulation

The activity is thought to be regulated mainly by the availability of decarboxylated S-adenosylmethionine. HAMAP-Rule MF_00198

Pathway

Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1. HAMAP-Rule MF_00198

Subunit structure

Homodimer. Ref.7 Ref.8

Sequence similarities

Belongs to the spermidine/spermine synthase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 10.4. HAMAP-Rule MF_00198

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 288287Spermidine synthase HAMAP-Rule MF_00198
PRO_0000156479

Regions

Region140 – 1412S-adenosylmethioninamine binding By similarity

Sites

Active site1581Proton acceptor By similarity
Binding site331S-adenosylmethioninamine By similarity
Binding site631Putrescine By similarity
Binding site881S-adenosylmethioninamine By similarity
Binding site1081S-adenosylmethioninamine By similarity
Binding site1611Putrescine By similarity
Binding site2261Putrescine By similarity

Secondary structure

................................................... 288
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09158 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 31AE026FF6199E9F

FASTA28832,321
        10         20         30         40         50         60 
MAEKKQWHET LHDQFGQYFA VDNVLYHEKT DHQDLIIFEN AAFGRVMALD GVVQTTERDE 

        70         80         90        100        110        120 
FIYHEMMTHV PLLAHGHAKH VLIIGGGDGA MLREVTRHKN VESITMVEID AGVVSFCRQY 

       130        140        150        160        170        180 
LPNHNAGSYD DPRFKLVIDD GVNFVNQTSQ TFDVIISDCT DPIGPGESLF TSAFYEGCKR 

       190        200        210        220        230        240 
CLNPGGIFVA QNGVCFLQQE EAIDSHRKLS HYFSDVGFYQ AAIPTYYGGI MTFAWATDND 

       250        260        270        280 
ALRHLSTEII QARFLASGLK CRYYNPAIHT AAFALPQYLQ DALASQPS 

« Hide

References

« Hide 'large scale' references
[1]"The speEspeD operon of Escherichia coli. Formation and processing of a proenzyme form of S-adenosylmethionine decarboxylase."
Tabor C.W., Tabor H.
J. Biol. Chem. 262:16037-16040(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
Fujita N., Mori H., Yura T., Ishihama A.
Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Spermidine biosynthesis in Escherichia coli: promoter and termination regions of the speED operon."
Xie Q.W., Tabor C.W., Tabor H.
J. Bacteriol. 171:4457-4465(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
[6]"Spermidine synthase of Escherichia coli: localization of the speE gene."
Tabor C.W., Tabor H., Xie Q.W.
Proc. Natl. Acad. Sci. U.S.A. 83:6040-6044(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-31.
[7]"Spermidine biosynthesis. Purification and properties of propylamine transferase from Escherichia coli."
Bowman W.H., Tabor C.W., Tabor H.
J. Biol. Chem. 248:2480-2486(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, SUBUNIT.
[8]"The crystal structure of Escherichia coli spermidine synthase SpeE reveals a unique substrate-binding pocket."
Zhou X., Chua T.K., Tkaczuk K.L., Bujnicki J.M., Sivaraman J.
J. Struct. Biol. 169:277-285(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02804 Genomic DNA. Translation: AAA24643.1.
U00096 Genomic DNA. Translation: AAC73232.1.
AP009048 Genomic DNA. Translation: BAB96695.1.
PIRSYECSD. A29778.
RefSeqNP_414663.1. NC_000913.2.
YP_488424.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3O4FX-ray2.90A/B/C/D/E/F/G/H1-288[»]
ProteinModelPortalP09158.
SMRP09158. Positions 4-287.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-10908N.
IntActP09158. 10 interactions.
MINTMINT-1231846.
STRING511145.b0121.

2D gel databases

SWISS-2DPAGEP09158.

Proteomic databases

PaxDbP09158.
PRIDEP09158.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73232; AAC73232; b0121.
BAB96695; BAB96695; BAB96695.
GeneID12933098.
947726.
KEGGecj:Y75_p0118.
eco:b0121.
PATRIC32115343. VBIEscCol129921_0123.

Organism-specific databases

EchoBASEEB0956.
EcoGeneEG10963. speE.

Phylogenomic databases

eggNOGCOG0421.
HOGENOMHOG000256146.
KOK00797.
OMAELWYTEK.
ProtClustDBPRK00811.

Enzyme and pathway databases

BioCycEcoCyc:SPERMIDINESYN-MONOMER.
ECOL316407:JW0117-MONOMER.
MetaCyc:SPERMIDINESYN-MONOMER.
UniPathwayUPA00248; UER00314.

Gene expression databases

GenevestigatorP09158.

Family and domain databases

HAMAPMF_00198. Spermidine_synth.
InterProIPR001045. Spermidine/spermine_synthase.
[Graphical view]
PANTHERPTHR11558. PTHR11558. 1 hit.
PfamPF01564. Spermine_synth. 1 hit.
[Graphical view]
TIGRFAMsTIGR00417. speE. 1 hit.
PROSITEPS01330. SPERMIDINE_SYNTHASE_1. 1 hit.
PS51006. SPERMIDINE_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSPEE_ECOLI
AccessionPrimary (citable) accession number: P09158
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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