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Identification
HMDB Protein ID HMDBP00217
Secondary Accession Numbers
  • 5449
  • HMDBP05053
Name Spermine synthase
Synonyms
  1. SPMSY
  2. Spermidine aminopropyltransferase
Gene Name SMS
Protein Type Enzyme
Biological Properties
General Function Involved in spermine synthase activity
Specific Function Catalyzes the production of spermine from spermidine and decarboxylated S-adenosylmethionine (dcSAM).
Pathways
  • Arginine and proline metabolism
  • beta-Alanine metabolism
  • Cysteine and methionine metabolism
  • Glutathione metabolism
  • Spermidine and Spermine Biosynthesis
  • spermine biosynthesis
Reactions
S-Adenosylmethioninamine + Spermidine → 5'-Methylthioadenosine + Spermine details
GO Classification
Biological Process
polyamine metabolic process
methionine metabolic process
spermine biosynthetic process
Cellular Component
cytosol
Function
catalytic activity
transferase activity
transferase activity, transferring alkyl or aryl (other than methyl) groups
spermine synthase activity
Molecular Function
spermidine synthase activity
spermine synthase activity
Process
metabolic process
cellular metabolic process
cellular amino acid derivative metabolic process
cellular biogenic amine metabolic process
polyamine metabolic process
polyamine biosynthetic process
spermine biosynthetic process
cellular amino acid and derivative metabolic process
Cellular Location Not Available
Gene Properties
Chromosome Location X
Locus Xp22.1
SNPs SMS
Gene Sequence
>1101 bp
ATGGCAGCAGCACGGCACAGCACGCTCGACTTCATGCTCGGCGCCAAAGCTGATGGTGAG
ACCATTCTAAAAGGCCTCCAGTCCATTTTCCAGGAGCAGGGGATGGCGGAGTCGGTGCAC
ACCTGGCAGGACCATGGCTATTTAGCAACCTACACAAACAAGAACGGCAGCTTTGCCAAT
TTGAGAATTTACCCACATGGATTGGTGTTGCTGGACCTTCAGAGTTATGATGGTGATGCG
CAAGGCAAAGAAGAGATCGACAGTATTTTGAACAAAGTAGAGGAAAGAATGAAAGAATTG
AGTCAGGACAGTACTGGGCGGGTGAAACGATTACCACCCATAGTGCGAGGAGGAGCCATC
GACAGATACTGGCCCACCGCCGACGGGCGCCTGGTTGAATATGACATAGATGAAGTGGTA
TATGACGAAGATTCACCTTATCAAAATATAAAAATTCTACACTCGAAGCAGTTTGGAAAT
ATTCTCATCCTTAGTGGGGATGTTAATTTGGCAGAGAGTGATTTGGCATATACCCGGGCC
ATCATGGGCAGTGGCAAAGAAGATTACACTGGCAAAGATGTACTCATTCTGGGAGGTGGA
GACGGAGGCATATTGTGTGAAATAGTCAAACTAAAACCAAAGATGGTCACTATGGTAGAG
ATTGACCAAATGGTGATTGATGGGTGTAAGAAATACATGCGAAAAACGTGTGGCGATGTC
TTAGACAATCTTAAAGGAGACTGCTATCAGGTTCTAATAGAAGACTGTATCCCGGTACTG
AAGAGGTACGCCAAAGAAGGGAGAGAATTTGATTATGTGATTAATGATTTGACAGCTGTT
CCAATCTCCACGTCTCCAGAAGAAGATTCCACATGGGAGTTTCTCAGACTGATTCTTGAC
CTCTCAATGAAAGTGTTGAAACAGGATGGGAAATATTTTACACAGGGGAACTGTGTCAAT
CTGACAGAAGCACTGTCGCTCTATGAAGAACAGCTGGGGCGCCTGTATTGTCCTGTGGAA
TTTTCAAAGGAGATCGTCTGTGTCCCTTCATACTTGGAATTGTGGGTATTTTACACTGTT
TGGAAGAAAGCTAAACCCTGA
Protein Properties
Number of Residues 366
Molecular Weight 35278.2
Theoretical pI 5.018
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Spermine synthase
MAAARHSTLDFMLGAKADGETILKGLQSIFQEQGMAESVHTWQDHGYLATYTNKNGSFAN
LRIYPHGLVLLDLQSYDGDAQGKEEIDSILNKVEERMKELSQDSTGRVKRLPPIVRGGAI
DRYWPTADGRLVEYDIDEVVYDEDSPYQNIKILHSKQFGNILILSGDVNLAESDLAYTRA
IMGSGKEDYTGKDVLILGGGDGGILCEIVKLKPKMVTMVEIDQMVIDGCKKYMRKTCGDV
LDNLKGDCYQVLIEDCIPVLKRYAKEGREFDYVINDLTAVPISTSPEEDSTWEFLRLILD
LSMKVLKQDGKYFTQGNCVNLTEALSLYEEQLGRLYCPVEFSKEIVCVPSYLELWVFYTV
WKKAKP
GenBank ID Protein 2198557
UniProtKB/Swiss-Prot ID P52788
UniProtKB/Swiss-Prot Entry Name SPSY_HUMAN
PDB IDs
GenBank Gene ID AD001528
GeneCard ID SMS
GenAtlas ID SMS
HGNC ID HGNC:11123
References
General References
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  7. Korhonen VP, Halmekyto M, Kauppinen L, Myohanen S, Wahlfors J, Keinanen T, Hyvonen T, Alhonen L, Eloranta T, Janne J: Molecular cloning of a cDNA encoding human spermine synthase. DNA Cell Biol. 1995 Oct;14(10):841-7. [PubMed:7546290 ]
  8. Grieff M, Whyte MP, Thakker RV, Mazzarella R: Sequence analysis of 139 kb in Xp22.1 containing spermine synthase and the 5' region of PEX. Genomics. 1997 Sep 1;44(2):227-31. [PubMed:9299240 ]
  9. Cason AL, Ikeguchi Y, Skinner C, Wood TC, Holden KR, Lubs HA, Martinez F, Simensen RJ, Stevenson RE, Pegg AE, Schwartz CE: X-linked spermine synthase gene (SMS) defect: the first polyamine deficiency syndrome. Eur J Hum Genet. 2003 Dec;11(12):937-44. [PubMed:14508504 ]
  10. Wu H, Min J, Zeng H, McCloskey DE, Ikeguchi Y, Loppnau P, Michael AJ, Pegg AE, Plotnikov AN: Crystal structure of human spermine synthase: implications of substrate binding and catalytic mechanism. J Biol Chem. 2008 Jun 6;283(23):16135-46. doi: 10.1074/jbc.M710323200. Epub 2008 Mar 26. [PubMed:18367445 ]