D6ZLN1 (D6ZLN1_STRP0) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Spermidine synthase RuleBase RU003837 HAMAP-Rule MF_00198
EC=2.5.1.16 RuleBase RU003837 HAMAP-Rule MF_00198

Alternative name(s):
Putrescine aminopropyltransferase HAMAP-Rule MF_00198
SPDSY HAMAP-Rule MF_00198

Gene names

Name:	speE HAMAP-Rule MF_00198
Ordered Locus Names:	HMPREF0837_11567

Organism

Streptococcus pneumoniae serotype A19 (strain TCH8431) [Complete proteome] [HAMAP] EMBL ADI69795.1

Taxonomic identifier

525381 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › Streptococcus pneumoniae

Protein attributes

Sequence length	286 AA.
Sequence status	Complete.
Protein existence	Inferred 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-Rule MF_00198
Catalytic activity	S-adenosylmethioninamine + putrescine = S-methyl-5'-thioadenosine + spermidine. RuleBase RU003837 HAMAP-Rule MF_00198
Pathway	Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1. HAMAP-Rule MF_00198
Subunit structure	Homodimer or homotetramer By similarity. HAMAP-Rule MF_00198
Sequence similarities	Belongs to the spermidine/spermine synthase family. RuleBase RU003836 HAMAP-Rule MF_00198

Ontologies

Keywords
Biological process	Polyamine biosynthesis HAMAP-Rule MF_00198 Spermidine biosynthesis RuleBase RU003837 HAMAP-Rule MF_00198
Molecular function	Transferase RuleBase RU003836 HAMAP-Rule MF_00198 EMBL ADI69795.1
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	spermidine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	spermidine synthase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Region	137 – 138	2	S-adenosylmethioninamine binding By similarity HAMAP-Rule MF_00198
Sites
	Active site	155	1	Proton acceptor By similarity HAMAP-Rule MF_00198
	Binding site	31	1	S-adenosylmethioninamine By similarity HAMAP-Rule MF_00198
	Binding site	61	1	Putrescine By similarity HAMAP-Rule MF_00198
	Binding site	86	1	S-adenosylmethioninamine By similarity HAMAP-Rule MF_00198
	Binding site	106	1	S-adenosylmethioninamine By similarity HAMAP-Rule MF_00198
	Binding site	158	1	Putrescine By similarity HAMAP-Rule MF_00198

Sequences

	Sequence		Length	Mass (Da)
	D6ZLN1 [UniParc]. Last modified August 10, 2010. Version 1. Checksum: 2131961004F6917F	FASTA	286	32,859
	10 20 30 40 50 60 MDLWFSEVHT PDVKLSLRTA KQLYAGKSEW QDIEVLDTPA FGKILILNGH VLFSDADDFV 70 80 90 100 110 120 YNEMTVHVPM AVHPNPKKVL VIGGGDGGVA QVLTLYPELE QIDIVEPDEM LVEVCREYFP 130 140 150 160 170 180 DFAAGLDDPR VTIYYQNGLR FLRNCEDDYD IIINDATDPF GHTEGLFTKE FYGNSYRALK 190 200 210 220 230 240 EDGIMIYQHG SPFFDEDESA CRSMHRKVNQ AFPISRVYQA HIPTSPAGYW LFGFASKKYH 250 260 270 280 PVKDFDKEGW KKRQLFTEYY TANLHVGAFM LPKYVEDILE EEEGKK

References

[1]

"A catalog of reference genomes from the human microbiome." Nelson K.E., Weinstock G.M., Highlander S.K., Worley K.C., Creasy H.H., Wortman J.R., Rusch D.B., Mitreva M., Sodergren E., Chinwalla A.T., Feldgarden M., Gevers D., Haas B.J., Madupu R., Ward D.V., Birren B.W., Gibbs R.A., Methe B. , Petrosino J.F., Strausberg R.L., Sutton G.G., White O.R., Wilson R.K., Durkin S., Giglio M.G., Gujja S., Howarth C., Kodira C.D., Kyrpides N., Mehta T., Muzny D.M., Pearson M., Pepin K., Pati A., Qin X., Yandava C., Zeng Q., Zhang L., Berlin A.M., Chen L., Hepburn T.A., Johnson J., McCorrison J., Miller J., Minx P., Nusbaum C., Russ C., Sykes S.M., Tomlinson C.M., Young S., Warren W.C., Badger J., Crabtree J., Markowitz V.M., Orvis J., Cree A., Ferriera S., Fulton L.L., Fulton R.S., Gillis M., Hemphill L.D., Joshi V., Kovar C., Torralba M., Wetterstrand K.A., Abouellleil A., Wollam A.M., Buhay C.J., Ding Y., Dugan S., FitzGerald M.G., Holder M., Hostetler J., Clifton S.W., Allen-Vercoe E., Earl A.M., Farmer C.N., Liolios K., Surette M.G., Xu Q., Pohl C., Wilczek-Boney K., Zhu D. Science 328:994-999(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TCH8431.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001993 Genomic DNA. Translation: ADI69795.1.
RefSeq	YP_003725009.1. NC_014251.1.
3D structure databases
ProteinModelPortal	D6ZLN1.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ADI69795; ADI69795; HMPREF0837_11567.
GeneID	9344826.
KEGG	snc:HMPREF0837_11567.
PATRIC	38264833. VBIStrPne36006_1555.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000256146.
KO	K00797.
OMA	HPTIVDG.
Enzyme and pathway databases
BioCyc	SPNE525381:GH2H-1602-MONOMER.
UniPathway	UPA00248; UER00314.
Family and domain databases
HAMAP	MF_00198. Spermidine_synth.
InterPro	IPR001045. Spermidine/spermine_synthase. [Graphical view]
PANTHER	PTHR11558. PTHR11558. 1 hit.
Pfam	PF01564. Spermine_synth. 1 hit. [Graphical view]
TIGRFAMs	TIGR00417. speE. 1 hit.
PROSITE	PS51006. SPERMIDINE_SYNTHASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

D6ZLN1_STRP0

Accession

Primary (citable) accession number: D6ZLN1

Entry history

Integrated into UniProtKB/TrEMBL:	August 10, 2010
Last sequence update:	August 10, 2010
Last modified:	May 29, 2013
This is version 24 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)