You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Human Metabolome Database.
Identification
HMDB Protein ID HMDBP00218
Secondary Accession Numbers
  • 5450
  • HMDBP05052
Name Spermidine synthase
Synonyms
  1. Putrescine aminopropyltransferase
  2. SPDSY
Gene Name SRM
Protein Type Enzyme
Biological Properties
General Function Involved in catalytic activity
Specific Function Catalyzes the production of spermidine from putrescine and decarboxylated S-adenosylmethionine (dcSAM). Has a strong preference for putrescine as substrate, and has very low activity towards 1,3-diaminopropane. Has extremely low activity towards spermidine.
Pathways
  • Arginine and proline metabolism
  • beta-Alanine metabolism
  • Cystathionine Beta-Synthase Deficiency
  • Cysteine and methionine metabolism
  • Glutathione metabolism
  • Glycine N-methyltransferase Deficiency
  • Homocystinuria-megaloblastic anemia due to defect in cobalamin metabolism, cblG complementation type
  • Hypermethioninemia
  • Methionine Adenosyltransferase Deficiency
  • Methionine Metabolism
  • Methylenetetrahydrofolate Reductase Deficiency (MTHFRD)
  • S-Adenosylhomocysteine (SAH) Hydrolase Deficiency
  • Spermidine and Spermine Biosynthesis
  • spermidine biosynthesis
Reactions
S-Adenosylmethioninamine + Putrescine → 5'-Methylthioadenosine + Spermidine details
S-Adenosylmethioninamine + Spermidine → 5'-Methylthioadenosine + Spermine details
S-Adenosylmethioninamine + Cadaverine → 5'-Methylthioadenosine + Aminopropylcadaverine details
GO Classification
Biological Process
small molecule metabolic process
spermidine biosynthetic process
Cellular Component
cytosol
Function
catalytic activity
Molecular Function
spermidine synthase activity
protein homodimerization activity
Cellular Location Not Available
Gene Properties
Chromosome Location 1
Locus 1p36-p22
SNPs SRM
Gene Sequence
>909 bp
ATGGAGCCCGGCCCCGACGGCCCCGCCGCCTCCGGCCCCGCCGCCATCCGCGAGGGCTGG
TTCCGCGAGACCTGCAGCCTGTGGCCCGGCCAGGCCCTGTCACTGCAGGTGGAGCAGCTG
CTCCACCACCGGCGCTCGCGCTACCAGGACATCCTCGTCTTCCGCAGTAAGACCTATGGC
AACGTGCTGGTGTTGGACGGTGTCATCCAGTGCACGGAGAGAGACGAGTTCTCCTACCAG
GAGATGATCGCCAACCTGCCTCTCTGCAGCCACCCCAACCCGCGAAAGGTGCTGATCATC
GGGGGCGGAGATGGAGGTGTCCTGCGGGAGGTGGTGAAGCACCCCTCCGTGGAGTCCGTG
GTCCAGTGTGAGATCGACGAGGATGTCATCCAAGTCTCCAAGAAGTTCCTGCCAGGCATG
GCCATTGGCTACTCTAGCTCGAAGCTGACCCTACATGTGGGTGACGGTTTTGAGTTCATG
AAACAGAATCAGGATGCCTTCGACGTGATCATCACTGACTCCTCAGACCCCATGGGCCCC
GCCGAAAGTCTCTTCAAGGAGTCCTATTACCAGCTCATGAAGACAGCCCTCAAGGAAGAT
GGTGTCCTCTGCTGCCAGGGCGAGTGCCAGTGGCTGCACCTGGACCTCATCAAGGAGATG
CGGCAGTTCTGCCAGTCCCTGTTCCCCGTGGTGGCCTATGCCTACTGCACCATCCCCACC
TACCCCAGCGGCCAGATCGGCTTCATGCTGTGCAGCAAGAACCCGAGCACGAACTTCCAG
GAGCCGGTGCAGCCGCTGACACAGCAGCAGGTGGCGCAGATGCAGCTGAAGTACTACAAC
TCCGACGTGCACCGCGCCGCCTTTGTGCTGCCCGAGTTTGCCCGCAAGGCCCTGAATGAT
GTGAGCTGA
Protein Properties
Number of Residues 302
Molecular Weight 33824.455
Theoretical pI 5.49
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Spermidine synthase
MEPGPDGPAASGPAAIREGWFRETCSLWPGQALSLQVEQLLHHRRSRYQDILVFRSKTYG
NVLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESV
VQCEIDEDVIQVSKKFLPGMAIGYSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMGP
AESLFKESYYQLMKTALKEDGVLCCQGECQWLHLDLIKEMRQFCQSLFPVVAYAYCTIPT
YPSGQIGFMLCSKNPSTNFQEPVQPLTQQQVAQMQLKYYNSDVHRAAFVLPEFARKALND
VS
GenBank ID Protein 56204109
UniProtKB/Swiss-Prot ID P19623
UniProtKB/Swiss-Prot Entry Name SPEE_HUMAN
PDB IDs
GenBank Gene ID AL109811
GeneCard ID SRM
GenAtlas ID SRM
HGNC ID HGNC:11296
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed:16710414 ]
  3. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  4. Wahlfors J, Alhonen L, Kauppinen L, Hyvonen T, Janne J, Eloranta TO: Human spermidine synthase: cloning and primary structure. DNA Cell Biol. 1990 Mar;9(2):103-10. [PubMed:2344393 ]
  5. Myohanen S, Kauppinen L, Wahlfors J, Alhonen L, Janne J: Human spermidine synthase gene: structure and chromosomal localization. DNA Cell Biol. 1991 Jul-Aug;10(6):467-74. [PubMed:2069720 ]