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
- Functionsagmatine aminopropyltransferase activity / cadaverine aminopropyltransferase activity / spermidine synthase activity / sym-norspermidine synthase activity / thermospermine synthase activityProcessesspermidine biosynthetic processComponentscytosol
- 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
- Spermine_synth (PF01564)
- 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
Resource Link UniProtKB ID Q9WZC2 UniProtKB Entry Name SPEE_THEMA GenBank Protein ID 4981177 GenBank Gene ID AE000512 - General References
- 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]
- 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]
- 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]
- 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]