Polyamine aminopropyltransferase

Details

Name
Polyamine aminopropyltransferase
Synonyms
  • PAPT
  • Putrescine aminopropyltransferase
  • SPDS
  • SPDSY
  • Spermidine synthase
Gene Name
speE
Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Amino acid sequence
>lcl|BSEQ0016519|Polyamine aminopropyltransferase
MRTLKELERELQPRQHLWYFEYYTGNNVGLFMKMNRVIYSGQSDIQRIDIFENPDLGVVF
ALDGITMTTEKDEFMYHEMLAHVPMFLHPNPKKVLIIGGGDGGTLREVLKHDSVEKAILC
EVDGLVIEAARKYLKQTSCGFDDPRAEIVIANGAEYVRKFKNEFDVIIIDSTDPTAGQGG
HLFTEEFYQACYDALKEDGVFSAETEDPFYDIGWFKLAYRRISKVFPITRVYLGFMTTYP
SGMWSYTFASKGIDPIKDFDPEKVRKFNKELKYYNEEVHVASFALPNFVKKELGLM
Number of residues
296
Molecular Weight
34141.845
Theoretical pI
5.13
GO Classification
Functions
agmatine aminopropyltransferase activity / cadaverine aminopropyltransferase activity / spermidine synthase activity / sym-norspermidine synthase activity / thermospermine synthase activity
Processes
spermidine biosynthetic process
Components
cytosol
General Function
Thermospermine synthase activity
Specific Function
Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine. It has lower affinity and lower activity towards 1,3-diaminopropane, cadaverine (1,5-diaminopentane), agmatine, norspermidine and spermidine (in vitro).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0016520|Polyamine aminopropyltransferase (speE)
GTGAGAACGTTGAAGGAACTGGAAAGGGAACTTCAGCCAAGACAGCACCTCTGGTACTTC
GAGTACTACACGGGAAACAACGTGGGTCTTTTCATGAAGATGAACCGCGTGATTTATTCA
GGACAGAGCGATATACAGAGGATCGACATCTTCGAAAACCCCGATCTCGGTGTGGTCTTC
GCACTCGATGGAATCACAATGACAACAGAGAAAGACGAGTTCATGTACCACGAGATGCTC
GCACACGTTCCCATGTTCCTTCATCCCAATCCGAAGAAGGTGCTCATCATCGGTGGTGGA
GATGGGGGAACGCTCAGAGAAGTCCTCAAGCACGATAGCGTAGAAAAAGCCATTCTCTGC
GAGGTCGATGGCCTCGTCATAGAAGCGGCGAGGAAATATCTGAAACAGACCTCCTGTGGT
TTCGACGATCCCAGAGCGGAGATCGTGATAGCAAACGGTGCCGAATACGTGAGGAAGTTC
AAAAACGAGTTCGACGTCATCATCATAGACTCCACGGACCCGACGGCGGGTCAGGGCGGG
CACCTCTTCACCGAGGAGTTCTACCAGGCCTGCTACGACGCATTGAAGGAAGACGGAGTC
TTCTCTGCAGAAACGGAGGATCCGTTCTACGACATCGGATGGTTCAAACTCGCCTACAGG
AGGATCAGCAAGGTCTTTCCGATTACAAGGGTTTACCTTGGTTTCATGACCACCTATCCC
TCCGGCATGTGGTCCTACACTTTCGCCTCCAAGGGAATAGACCCGATAAAAGACTTCGAC
CCGGAAAAGGTGAGAAAGTTCAACAAAGAACTGAAGTACTACAACGAAGAAGTCCACGTT
GCCTCCTTTGCCCTCCCGAATTTCGTGAAGAAAGAACTCGGACTGATGTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDQ9WZC2
UniProtKB Entry NameSPEE_THEMA
GenBank Protein ID4981177
GenBank Gene IDAE000512
General References
  1. Nelson KE, Clayton RA, Gill SR, Gwinn ML, Dodson RJ, Haft DH, Hickey EK, Peterson JD, Nelson WC, Ketchum KA, McDonald L, Utterback TR, Malek JA, Linher KD, Garrett MM, Stewart AM, Cotton MD, Pratt MS, Phillips CA, Richardson D, Heidelberg J, Sutton GG, Fleischmann RD, Eisen JA, White O, Salzberg SL, Smith HO, Venter JC, Fraser CM: Evidence for lateral gene transfer between Archaea and bacteria from genome sequence of Thermotoga maritima. Nature. 1999 May 27;399(6734):323-9. [Article]
  2. Pegg AE, Poulin R, Coward JK: Use of aminopropyltransferase inhibitors and of non-metabolizable analogs to study polyamine regulation and function. Int J Biochem Cell Biol. 1995 May;27(5):425-42. [Article]
  3. 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]
  4. Korolev S, Ikeguchi Y, Skarina T, Beasley S, Arrowsmith C, Edwards A, Joachimiak A, Pegg AE, Savchenko A: The crystal structure of spermidine synthase with a multisubstrate adduct inhibitor. Nat Struct Biol. 2002 Jan;9(1):27-31. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02844S-Adenosyl-1,8-Diamino-3-ThiooctaneexperimentalunknownDetails