Reviewed, UniProtKB/Swiss-Prot Q9SC13 (HSS1_SENVE)

Names and origin

Protein names

Recommended name:
    Homospermidine synthase 1
    EC=2.5.1.45

Gene names

Name:

HSS1

Organism

Senecio vernalis (Spring groundsel)

Taxonomic identifier

93496 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › campanulids › Asterales › Asteraceae › Asteroideae › Senecioneae › Senecio

Protein attributes

Sequence length	370 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the transfer of an aminobutyl unit from spermidine onto putrescine. The resulting polyamine homospermidine is a precursor in the biosynthesis of pyrrolizidine alkaloids.
Catalytic activity	Spermidine + putrescine = sym-homospermidine + propane-1,3-diamine.
Cofactor	NAD.
Pathway	Alkaloid biosynthesis; pyrrolizidine alkaloid biosynthesis.
Subunit structure	Homotetramer.
Tissue specificity	Expressed in roots.
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Belongs to the deoxyhypusine synthase family.
Caution	Sequence shown in Ref.1 correspond to the product of the second gene cited in Ref.2.

Ontologies

Keywords
Ligand	NAD
Molecular function	Transferase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	peptidyl-lysine modification to hypusine Inferred from electronic annotation. Source: InterPro
Molecular function	homospermidine synthase (spermidine-specific) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 370	370	Homospermidine synthase 1		PRO_0000134517

Sequences

	Sequence		Length	Mass (Da)
	Q9SC13-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 5E81E09C5A3A8689	FASTA	370	40,726
	10 20 30 40 50 60 MAESNKEAID SARSNVFKES ESLEGTCAKI GGYDFNNGID HSKLLKSMVS TGFQASNLGD 70 80 90 100 110 120 AMIITNQMLD WRLSHDEVPE NCSEEEKKNR ESVKCKIFLG FTSNLISSGV RETICYLTQH 130 140 150 160 170 180 RMVDVLVTTT GGIEEDFIKC LASTYKGKFS LPGADLRSKG LNRIGNLIVP NDNYIKFEDW 190 200 210 220 230 240 IIPIFDQMLI EQKTQNVLWT PSRMIARLGK EINNETSYLY WAYKNNIPVF CPSITDGSIG 250 260 270 280 290 300 DMLYFHSVSN PGPGLVVDIV QDVIAMDNEA VHASPQKTGI IILGGGLPKH HICNANMMRN 310 320 330 340 350 360 GADFAVFINT AQEYDGSDSG ARPDEAVSWG KISSTGKAVK VHCDATIAFP LLVAETFAVK 370 KEKASKVNGF

References

[1]	"Homospermidine synthase, the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, evolved from deoxyhypusine synthase." Ober D., Hartmann T. Proc. Natl. Acad. Sci. U.S.A. 96:14777-14782(1999) [PubMed: 10611289] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 7-17; 151-159; 211-224 AND 278-289. Tissue: Root.
[2]	"Cloning and expression of homospermidine synthase from Senecio vulgaris: a revision." Ober D., Harms R., Hartmann T. Phytochemistry 55:305-309(2000) [PubMed: 11117877] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ238623 mRNA. Translation: CAB65462.1.
3D structure databases
SMR	Q9SC13. Positions 29-362.
ModBase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-13926.
BRENDA	2.5.1.45. 267997.
Family and domain databases
InterPro	IPR002773. Deoxyhypus_synth. [Graphical view]
Gene3D	G3DSA:3.40.910.10. Deoxyhypus_synth. 1 hit.
PANTHER	PTHR11703. Deoxyhypus_synth. 1 hit.
Pfam	PF01916. DS. 1 hit. [Graphical view]
TIGRFAMs	TIGR00321. dhys. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HSS1_SENVE

Accession

Primary (citable) accession number: Q9SC13

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 21, 2003
Last sequence update:	May 1, 2000
Last modified:	February 9, 2010
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)