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Q9PH03 (SPEE_XYLFA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:XF_0143
OrganismXylella fastidiosa [Complete proteome] [HAMAP]
Taxonomic identifier2371 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xylella

Protein attributes

Sequence length285 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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. HAMAP MF_00198

Subunit structure

Homodimer and homotetramer By similarity. HAMAP MF_00198

Sequence similarities

Belongs to the spermidine/spermine synthase family.

Ontologies

Keywords
   Biological processPolyamine biosynthesis
Spermidine biosynthesis
   Molecular functionTransferase
   Technical termComplete 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 – 285285Spermidine synthase HAMAP MF_00198
PRO_0000156521

Regions

Region141 – 1422S-adenosylmethioninamine binding By similarity

Sites

Active site1601Proton acceptor By similarity
Binding site351S-adenosylmethioninamine By similarity
Binding site651Putrescine By similarity
Binding site901S-adenosylmethioninamine By similarity
Binding site1101S-adenosylmethioninamine By similarity
Binding site1631Putrescine By similarity
Binding site2291Putrescine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PH03 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: F2EAD07859DA9D50

FASTA28531,907
        10         20         30         40         50         60 
MTTNDSWFTE HFQATGSAIG FRITGKLDEV QSPFQKIEIY NSTDWGKLMV IDGALMLTSR 

        70         80         90        100        110        120 
DNFLYHEMIS HPALFTHTAP KCVVIIGGGD CGTLREVLKH PDIEQVTQCD IDEQVTRMAE 

       130        140        150        160        170        180 
KHFPELCTSN NDPRATLLFS DGVAYMTDCP TNSVDVIIVD STDPVGPAKG LFNRTFYESC 

       190        200        210        220        230        240 
FRALKNDGLL VQQSESPLAL LELIKEMRHE MSKAGFKAFK TLPFPQPCYP TGWWSVTLSS 

       250        260        270        280 
KQPNANFAFR QTDAQTKPFD TLYYNAHLHH GVLVPPPFIA HALGE

« Hide

References

[1]"The genome sequence of the plant pathogen Xylella fastidiosa."
Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., Bueno M.R.P., Camargo A.A., Camargo L.E.A. expand/collapse author list , Carraro D.M., Carrer H., Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M., Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S., Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H., Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F., Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N., Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F., Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y., Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O., Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A., de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R., Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B., Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M., da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z., Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.
Nature 406:151-159(2000) [PubMed: 10910347] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 9a5c.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE003849 Genomic DNA. Translation: AAF82956.1.
PIRB82842.
RefSeqNP_297436.1. NC_002488.3.

3D structure databases

ProteinModelPortalQ9PH03.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1125661.
GenomeReviewsGene locus XF_0143 in contig AE003849_GR.
KEGGxfa:XF0143.
NMPDRfig|160492.1.peg.143.
PATRIC24130190. VBIXylFas578_0152.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG635113.
OMAWFTEYHN.
ProtClustDBPRK00811.

Enzyme and pathway databases

BioCycXFAS160492:XF0143-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_XYLFA
AccessionPrimary (citable) accession number: Q9PH03
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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