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Polyamine aminopropyltransferase (AdoMetDC) (SAMDC) (EC 4.1.1.50) (Putrescine aminopropyltransferase) (S-adenosylmethionine decarboxylase proenzyme) (Spermidine synthase) (PAPT) (SPDS) (SPDSY) (EC 2.5.1.16) [Cleaved into: S-adenosylmethionine decarboxylase alpha chain; S-adenosylmethionine decarboxylase beta chain]

 A0A1Q8L0S9_9PSEU        Unreviewed;       430 AA.
A0A1Q8L0S9;
12-APR-2017, integrated into UniProtKB/TrEMBL.
12-APR-2017, sequence version 1.
22-NOV-2017, entry version 7.
RecName: Full=Polyamine aminopropyltransferase {ECO:0000256|HAMAP-Rule:MF_00198};
Short=AdoMetDC {ECO:0000256|HAMAP-Rule:MF_00464};
Short=SAMDC {ECO:0000256|HAMAP-Rule:MF_00464};
EC=4.1.1.50 {ECO:0000256|HAMAP-Rule:MF_00464};
AltName: Full=Putrescine aminopropyltransferase {ECO:0000256|HAMAP-Rule:MF_00198};
AltName: Full=S-adenosylmethionine decarboxylase proenzyme {ECO:0000256|HAMAP-Rule:MF_00464};
AltName: Full=Spermidine synthase {ECO:0000256|HAMAP-Rule:MF_00198};
Short=PAPT {ECO:0000256|HAMAP-Rule:MF_00198};
Short=SPDS {ECO:0000256|HAMAP-Rule:MF_00198};
Short=SPDSY {ECO:0000256|HAMAP-Rule:MF_00198};
EC=2.5.1.16 {ECO:0000256|HAMAP-Rule:MF_00198};
Contains:
RecName: Full=S-adenosylmethionine decarboxylase alpha chain {ECO:0000256|HAMAP-Rule:MF_00464};
Contains:
RecName: Full=S-adenosylmethionine decarboxylase beta chain {ECO:0000256|HAMAP-Rule:MF_00464};
Name=speE {ECO:0000256|HAMAP-Rule:MF_00198};
Synonyms=speH {ECO:0000256|HAMAP-Rule:MF_00464};
ORFNames=Ae706Ps2_0808 {ECO:0000313|EMBL:OLM22376.1};
Pseudonocardia sp. Ae706_Ps2.
Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
Pseudonocardia.
NCBI_TaxID=1885035 {ECO:0000313|EMBL:OLM22376.1, ECO:0000313|Proteomes:UP000186755};
[1] {ECO:0000313|EMBL:OLM22376.1, ECO:0000313|Proteomes:UP000186755}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Ae706_Ps2 {ECO:0000313|EMBL:OLM22376.1,
ECO:0000313|Proteomes:UP000186755};
Holmes N.A., Innocent T.M., Heine D., Al Bassam M., Worsley S.F.,
Trottmann F., Patrick E.H., Yu D.W., Murrell J.C., Schioett M.,
Wilkinson B., Boomsma J., Hutchings M.I.;
"Genome Analysis of Two Pseudonocardia Phylotypes Associated with
Acromyrmex Leafcutter Ants Reveals Their Biosynthetic Potential.";
Front. Microbiol. 7:1-16(2016).
-!- FUNCTION: Catalyzes the decarboxylation of S-adenosylmethionine to
S-adenosylmethioninamine (dcAdoMet), the propylamine donor
required for the synthesis of the polyamines spermine and
spermidine from the diamine putrescine. {ECO:0000256|HAMAP-
Rule:MF_00464}.
-!- 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.
{ECO:0000256|HAMAP-Rule:MF_00198}.
-!- CATALYTIC ACTIVITY: S-adenosyl 3-(methylthio)propylamine +
putrescine = 5'-S-methyl-5'-thioadenosine + spermidine.
{ECO:0000256|HAMAP-Rule:MF_00198}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = S-adenosyl 3-
(methylthio)propylamine + CO(2). {ECO:0000256|HAMAP-
Rule:MF_00464}.
-!- COFACTOR:
Name=pyruvate; Xref=ChEBI:CHEBI:15361;
Evidence={ECO:0000256|HAMAP-Rule:MF_00464};
Note=Binds 1 pyruvoyl group covalently per subunit.
{ECO:0000256|HAMAP-Rule:MF_00464};
-!- PATHWAY: Amine and polyamine biosynthesis; S-
adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from
S-adenosyl-L-methionine: step 1/1. {ECO:0000256|HAMAP-
Rule:MF_00464}.
-!- PATHWAY: Amine and polyamine biosynthesis; spermidine
biosynthesis; spermidine from putrescine: step 1/1.
{ECO:0000256|HAMAP-Rule:MF_00198}.
-!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged
as a dimer of alpha/beta heterodimers. {ECO:0000256|HAMAP-
Rule:MF_00464}.
-!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP-
Rule:MF_00198}.
-!- PTM: Is synthesized initially as an inactive proenzyme. Formation
of the active enzyme involves a self-maturation process in which
the active site pyruvoyl group is generated from an internal
serine residue via an autocatalytic post-translational
modification. Two non-identical subunits are generated from the
proenzyme in this reaction, and the pyruvate is formed at the N-
terminus of the alpha chain, which is derived from the carboxyl
end of the proenzyme. The post-translation cleavage follows an
unusual pathway, termed non-hydrolytic serinolysis, in which the
side chain hydroxyl group of the serine supplies its oxygen atom
to form the C-terminus of the beta chain, while the remainder of
the serine residue undergoes an oxidative deamination to produce
ammonia and the pyruvoyl group blocking the N-terminus of the
alpha chain. {ECO:0000256|HAMAP-Rule:MF_00464}.
-!- SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 1
subfamily. {ECO:0000256|HAMAP-Rule:MF_00464}.
-!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
{ECO:0000256|HAMAP-Rule:MF_00198}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00198}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:OLM22376.1}.
-----------------------------------------------------------------------
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EMBL; MCIQ01000001; OLM22376.1; -; Genomic_DNA.
UniPathway; UPA00248; UER00314.
UniPathway; UPA00331; UER00451.
Proteomes; UP000186755; Unassembled WGS sequence.
GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:UniProtKB-UniRule.
GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-UniRule.
GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
Gene3D; 3.60.90.10; -; 1.
HAMAP; MF_00464; AdoMetDC_1; 1.
HAMAP; MF_00198; Spermidine_synth; 1.
InterPro; IPR003826; AdoMetDC_fam_prok.
InterPro; IPR030374; PABS.
InterPro; IPR016067; S-AdoMet_deCO2ase_core.
InterPro; IPR017716; S-AdoMet_deCOase_pro-enz.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR001045; Spermi_synthase.
Pfam; PF02675; AdoMet_dc; 1.
SUPFAM; SSF53335; SSF53335; 1.
SUPFAM; SSF56276; SSF56276; 1.
TIGRFAMs; TIGR03330; SAM_DCase_Bsu; 1.
PROSITE; PS51006; PABS_2; 1.
3: Inferred from homology;
Autocatalytic cleavage {ECO:0000256|HAMAP-Rule:MF_00464};
Complete proteome {ECO:0000313|Proteomes:UP000186755};
Decarboxylase {ECO:0000256|HAMAP-Rule:MF_00464};
Lyase {ECO:0000256|HAMAP-Rule:MF_00464};
Polyamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00198,
ECO:0000256|PROSITE-ProRule:PRU00354};
Pyruvate {ECO:0000256|HAMAP-Rule:MF_00464};
S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00464};
Schiff base {ECO:0000256|HAMAP-Rule:MF_00464};
Spermidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00198};
Transferase {ECO:0000256|HAMAP-Rule:MF_00198, ECO:0000256|PROSITE-
ProRule:PRU00354, ECO:0000313|EMBL:OLM22376.1};
Zymogen {ECO:0000256|HAMAP-Rule:MF_00464}.
DOMAIN 143 386 PABS. {ECO:0000259|PROSITE:PS51006}.
REGION 283 284 S-adenosylmethioninamine binding.
{ECO:0000256|HAMAP-Rule:MF_00198}.
ACT_SITE 90 90 Schiff-base intermediate with substrate;
via pyruvic acid. {ECO:0000256|HAMAP-
Rule:MF_00464}.
ACT_SITE 95 95 Proton acceptor; for processing activity.
{ECO:0000256|HAMAP-Rule:MF_00464}.
ACT_SITE 110 110 Proton donor; for catalytic activity.
{ECO:0000256|HAMAP-Rule:MF_00464}.
ACT_SITE 301 301 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_00198, ECO:0000256|PROSITE-
ProRule:PRU00354}.
BINDING 148 148 Polyamine. {ECO:0000256|HAMAP-
Rule:MF_00198}.
BINDING 172 172 S-adenosylmethioninamine.
{ECO:0000256|HAMAP-Rule:MF_00198}.
BINDING 202 202 Polyamine. {ECO:0000256|HAMAP-
Rule:MF_00198}.
BINDING 226 226 Polyamine. {ECO:0000256|HAMAP-
Rule:MF_00198}.
BINDING 245 245 S-adenosylmethioninamine.
{ECO:0000256|HAMAP-Rule:MF_00198}.
SITE 89 90 Cleavage (non-hydrolytic); by autolysis.
{ECO:0000256|HAMAP-Rule:MF_00464}.
MOD_RES 90 90 Pyruvic acid (Ser); by autocatalysis.
{ECO:0000256|HAMAP-Rule:MF_00464}.
SEQUENCE 430 AA; 46106 MW; A9182DE36C8DCB40 CRC64;
MSVPATAAGE LHPGTGLGTG APALPSTSSP VGRHVLAELG GIAPEILDDC ARLRSDLTAA
LTEAGAQVRQ VVVERFEPQG ATVVAVLAES HASIHTWPEH GGMHVDVFTC GESADPVDAV
RRLADRVGAT DTALQVVDRG GAPRTVTEPL SPGLTRRWDL GRVHHVADTG FQHVVVADTA
HGVTLFCDDE RQSTEHTQLT YHEALVWPGA LLARELDRVL IIGSSEGVAS EMAVAAGASR
VDHVDIDAEA VRICAEHLPY GYTPESLAAA ERGEGPVHLT YGDGRQFVLD AREHWDLVIV
DLPDERPDVP DAQINRLYEE EFVRACAQRL TPGGVLVFQA GSPAVWRDAT LRSAWQRFAA
VFGETGGRGV YIGCEEHEWA FLAGVREPMA DPGAVAAERL ASMPLQPQLW DATALRHRLV
APLSLRRLTD


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