Spermidine synthase

Details

Name
Spermidine synthase
Synonyms
  • 2.5.1.16
  • Putrescine aminopropyltransferase
  • SPDSY
  • SPS1
  • SRML1
Gene Name
SRM
Organism
Humans
Amino acid sequence
>lcl|BSEQ0010239|Spermidine synthase
MEPGPDGPAASGPAAIREGWFRETCSLWPGQALSLQVEQLLHHRRSRYQDILVFRSKTYG
NVLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESV
VQCEIDEDVIQVSKKFLPGMAIGYSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMGP
AESLFKESYYQLMKTALKEDGVLCCQGECQWLHLDLIKEMRQFCQSLFPVVAYAYCTIPT
YPSGQIGFMLCSKNPSTNFQEPVQPLTQQQVAQMQLKYYNSDVHRAAFVLPEFARKALND
VS
Number of residues
302
Molecular Weight
33824.455
Theoretical pI
5.17
GO Classification
Functions
protein homodimerization activity / spermidine synthase activity
Processes
cellular nitrogen compound metabolic process / polyamine metabolic process / small molecule metabolic process / spermidine biosynthetic process
Components
cytosol
General Function
Spermidine synthase 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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0010240|Spermidine synthase (SRM)
ATGGAGCCCGGCCCCGACGGCCCCGCCGCCTCCGGCCCCGCCGCCATCCGCGAGGGCTGG
TTCCGCGAGACCTGCAGCCTGTGGCCCGGCCAGGCCCTGTCACTGCAGGTGGAGCAGCTG
CTCCACCACCGGCGCTCGCGCTACCAGGACATCCTCGTCTTCCGCAGTAAGACCTATGGC
AACGTGCTGGTGTTGGACGGTGTCATCCAGTGCACGGAGAGAGACGAGTTCTCCTACCAG
GAGATGATCGCCAACCTGCCTCTCTGCAGCCACCCCAACCCGCGAAAGGTGCTGATCATC
GGGGGCGGAGATGGAGGTGTCCTGCGGGAGGTGGTGAAGCACCCCTCCGTGGAGTCCGTG
GTCCAGTGTGAGATCGACGAGGATGTCATCCAAGTCTCCAAGAAGTTCCTGCCAGGCATG
GCCATTGGCTACTCTAGCTCGAAGCTGACCCTACATGTGGGTGACGGTTTTGAGTTCATG
AAACAGAATCAGGATGCCTTCGACGTGATCATCACTGACTCCTCAGACCCCATGGGCCCC
GCCGAAAGTCTCTTCAAGGAGTCCTATTACCAGCTCATGAAGACAGCCCTCAAGGAAGAT
GGTGTCCTCTGCTGCCAGGGCGAGTGCCAGTGGCTGCACCTGGACCTCATCAAGGAGATG
CGGCAGTTCTGCCAGTCCCTGTTCCCCGTGGTGGCCTATGCCTACTGCACCATCCCCACC
TACCCCAGCGGCCAGATCGGCTTCATGCTGTGCAGCAAGAACCCGAGCACGAACTTCCAG
GAGCCGGTGCAGCCGCTGACACAGCAGCAGGTGGCGCAGATGCAGCTGAAGTACTACAAC
TCCGACGTGCACCGCGCCGCCTTTGTGCTGCCCGAGTTTGCCCGCAAGGCCCTGAATGAT
GTGAGCTGA
Chromosome Location
1
Locus
1p36-p22
External Identifiers
ResourceLink
UniProtKB IDP19623
UniProtKB Entry NameSPEE_HUMAN
GenBank Protein ID531202
GenBank Gene IDM34338
GenAtlas IDSRM
HGNC IDHGNC:11296
General References
  1. 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. [Article]
  2. 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. [Article]
  3. 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. [Article]
  4. 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. [Article]
  5. 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. [Article]
  6. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  7. Bienvenut WV, Sumpton D, Martinez A, Lilla S, Espagne C, Meinnel T, Giglione C: Comparative large scale characterization of plant versus mammal proteins reveals similar and idiosyncratic N-alpha-acetylation features. Mol Cell Proteomics. 2012 Jun;11(6):M111.015131. doi: 10.1074/mcp.M111.015131. Epub 2012 Jan 5. [Article]
  8. Van Damme P, Lasa M, Polevoda B, Gazquez C, Elosegui-Artola A, Kim DS, De Juan-Pardo E, Demeyer K, Hole K, Larrea E, Timmerman E, Prieto J, Arnesen T, Sherman F, Gevaert K, Aldabe R: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. Proc Natl Acad Sci U S A. 2012 Jul 31;109(31):12449-54. doi: 10.1073/pnas.1210303109. Epub 2012 Jul 18. [Article]
  9. Wu H, Min J, Ikeguchi Y, Zeng H, Dong A, Loppnau P, Pegg AE, Plotnikov AN: Structure and mechanism of spermidine synthases. Biochemistry. 2007 Jul 17;46(28):8331-9. Epub 2007 Jun 22. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00118Ademetionineapproved, investigational, nutraceuticalunknownsubstrateDetails