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P70998 (SPEE_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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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
Synonyms:ywhF
Ordered Locus Names:BSU37500
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length276 AA.
Sequence statusComplete.
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 By similarity. HAMAP MF_00198

Catalytic activity

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

Pathway

Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1. Ref.3

Subunit structure

Homodimer or homotetramer. Ref.4

Sequence similarities

Belongs to the spermidine/spermine synthase family.

Ontologies

Keywords
   Biological processPolyamine biosynthesis
Spermidine biosynthesis
   Molecular functionTransferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processspermidine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionspermidine synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 276276Spermidine synthase HAMAP MF_00198
PRO_0000156470

Regions

Region138 – 1392S-adenosylmethioninamine binding By similarity

Sites

Active site1561Proton acceptor By similarity
Binding site321S-adenosylmethioninamine By similarity
Binding site621Putrescine By similarity
Binding site871S-adenosylmethioninamine By similarity
Binding site1071S-adenosylmethioninamine By similarity
Binding site1591Putrescine By similarity
Binding site2241Putrescine By similarity

Secondary structure

1 .................................................. 276
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P70998 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: A5E0725B80FBDD62

FASTA27631,336
        10         20         30         40         50         60 
MSELWYTEKQ TKNFGITMKV NKTLHTEQTE FQHLEMVETE EFGNMLFLDG MVMTSEKDEF 

        70         80         90        100        110        120 
VYHEMVAHVP LFTHPNPEHV LVVGGGDGGV IREILKHPSV KKATLVDIDG KVIEYSKKFL 

       130        140        150        160        170        180 
PSIAGKLDDP RVDVQVDDGF MHIAKSENQY DVIMVDSTEP VGPAVNLFTK GFYAGIAKAL 

       190        200        210        220        230        240 
KEDGIFVAQT DNPWFTPELI TNVQRDVKEI FPITKLYTAN IPTYPSGLWT FTIGSKKYDP 

       250        260        270 
LAVEDSRFFD IETKYYTKDI HKAAFVLPKF VSDLIK

« Hide

References

« Hide 'large scale' references
[1]"The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees)."
Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V., Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G., Kunst F., Danchin A., Glaser P.
Microbiology 143:3313-3328(1997) [PubMed: 9353933] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Characterization of polyamine synthesis pathway in Bacillus subtilis 168."
Sekowska A., Bertin P., Danchin A.
Mol. Microbiol. 29:851-858(1998) [PubMed: 9723923] [Abstract]
Cited for: CHARACTERIZATION OF POLYAMINE PATHWAY.
[4]"Crystal structure of spermidine synthase."
Northeast structural genomics consortium (NESG)
Submitted (JAN-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-276, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z80360 Genomic DNA. Translation: CAB02516.1.
AL009126 Genomic DNA. Translation: CAB15777.1.
PIRG70057.
RefSeqNP_391630.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IY9X-ray2.30A/B/C/D2-276[»]
ProteinModelPortalP70998.
SMRP70998. Positions 2-275.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000003280; EBBACP00000003280; EBBACG00000003273.
GeneID937075.
GenomeReviewsGene locus BSU37500 in contig AL009126_GR.
KEGGbsu:BSU37500.
NMPDRfig|224308.1.peg.3756.
PATRIC18979536. VBIBacSub10457_3930.

Organism-specific databases

GenoListBSU37500. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000002486.
HOGENOMHBG635113.
OMAELWYTEK.
PhylomeDBP70998.
ProtClustDBPRK00811.

Enzyme and pathway databases

BioCycBSUB:BSU37500-MONOMER.

Family and domain databases

HAMAPMF_00198. Spermidine_synth.
[Tree]
InterProIPR001045. Sprmine_synthase.
[Graphical view]
KOK00797.
PANTHERPTHR11558. Sprmine_synthase. 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_BACSU
AccessionPrimary (citable) accession number: P70998
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: February 1, 1997
Last modified: January 25, 2012
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

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

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