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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]

 A0A0N8KNC2_9CYAN        Unreviewed;       431 AA.
A0A0N8KNC2;
20-JAN-2016, integrated into UniProtKB/TrEMBL.
20-JAN-2016, sequence version 1.
25-OCT-2017, entry version 20.
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,
ECO:0000313|EMBL:KPQ36130.1};
Synonyms=speH {ECO:0000256|HAMAP-Rule:MF_00464};
ORFNames=HLUCCA11_07920 {ECO:0000313|EMBL:KPQ36130.1};
Phormidesmis priestleyi Ana.
Bacteria; Cyanobacteria; Synechococcales; Leptolyngbyaceae;
Phormidesmis.
NCBI_TaxID=1666911 {ECO:0000313|EMBL:KPQ36130.1, ECO:0000313|Proteomes:UP000050465};
[1] {ECO:0000313|EMBL:KPQ36130.1, ECO:0000313|Proteomes:UP000050465}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Ana {ECO:0000313|EMBL:KPQ36130.1};
Nelson W.C., Romine M.F., Lindemann S.R.;
"Identification and resolution of microdiversity through metagenomic
sequencing of parallel consortia.";
Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
-!- 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, ECO:0000256|SAAS:SAAS00639695}.
-!- 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, ECO:0000256|RuleBase:RU003837}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = S-adenosyl 3-
(methylthio)propylamine + CO(2). {ECO:0000256|HAMAP-Rule:MF_00464,
ECO:0000256|SAAS:SAAS00639698}.
-!- 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, ECO:0000256|SAAS:SAAS00639657}.
-!- 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}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00931765}.
-!- 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, ECO:0000256|RuleBase:RU003836}.
-!- 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:KPQ36130.1}.
-----------------------------------------------------------------------
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EMBL; LJZR01000008; KPQ36130.1; -; Genomic_DNA.
EnsemblBacteria; KPQ36130; KPQ36130; HLUCCA11_07920.
PATRIC; fig|1666911.3.peg.3895; -.
UniPathway; UPA00248; UER00314.
UniPathway; UPA00331; UER00451.
Proteomes; UP000050465; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 2.30.140.10; -; 1.
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; IPR030373; PABS_CS.
InterPro; IPR016067; S-AdoMet_deCO2ase_core.
InterPro; IPR017716; S-AdoMet_deCOase_pro-enz.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR001045; Spermi_synthase.
InterPro; IPR035246; Spermidine_synt_N.
InterPro; IPR037163; Spermidine_synt_N_sf.
Pfam; PF02675; AdoMet_dc; 1.
Pfam; PF17284; Spermine_synt_N; 1.
SUPFAM; SSF53335; SSF53335; 1.
SUPFAM; SSF56276; SSF56276; 1.
TIGRFAMs; TIGR03330; SAM_DCase_Bsu; 1.
TIGRFAMs; TIGR00417; speE; 1.
PROSITE; PS01330; PABS_1; 1.
PROSITE; PS51006; PABS_2; 1.
3: Inferred from homology;
Autocatalytic cleavage {ECO:0000256|HAMAP-Rule:MF_00464};
Complete proteome {ECO:0000313|Proteomes:UP000050465};
Cytoplasm {ECO:0000256|SAAS:SAAS00931762};
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};
Reference proteome {ECO:0000313|Proteomes:UP000050465};
S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00464,
ECO:0000256|SAAS:SAAS00639675};
Schiff base {ECO:0000256|HAMAP-Rule:MF_00464};
Spermidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00198,
ECO:0000256|RuleBase:RU003837, ECO:0000256|SAAS:SAAS00639670};
Transferase {ECO:0000256|HAMAP-Rule:MF_00198, ECO:0000256|PROSITE-
ProRule:PRU00354, ECO:0000256|RuleBase:RU003836};
Zymogen {ECO:0000256|HAMAP-Rule:MF_00464}.
DOMAIN 144 384 PABS. {ECO:0000259|PROSITE:PS51006}.
REGION 283 284 S-adenosylmethioninamine binding.
{ECO:0000256|HAMAP-Rule:MF_00198}.
REGION 303 305 Polyamine binding. {ECO:0000256|HAMAP-
Rule:MF_00198}.
ACT_SITE 63 63 Schiff-base intermediate with substrate;
via pyruvic acid. {ECO:0000256|HAMAP-
Rule:MF_00464}.
ACT_SITE 68 68 Proton acceptor; for processing activity.
{ECO:0000256|HAMAP-Rule:MF_00464}.
ACT_SITE 83 83 Proton donor; for catalytic activity.
{ECO:0000256|HAMAP-Rule:MF_00464}.
ACT_SITE 302 302 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_00198, ECO:0000256|PROSITE-
ProRule:PRU00354}.
BINDING 149 149 Polyamine. {ECO:0000256|HAMAP-
Rule:MF_00198}.
BINDING 173 173 S-adenosylmethioninamine.
{ECO:0000256|HAMAP-Rule:MF_00198}.
BINDING 204 204 Polyamine. {ECO:0000256|HAMAP-
Rule:MF_00198}.
BINDING 232 232 Polyamine. {ECO:0000256|HAMAP-
Rule:MF_00198}.
BINDING 252 252 S-adenosylmethioninamine.
{ECO:0000256|HAMAP-Rule:MF_00198}.
BINDING 309 309 S-adenosylmethioninamine; via carbonyl
oxygen. {ECO:0000256|HAMAP-
Rule:MF_00198}.
SITE 62 63 Cleavage (non-hydrolytic); by autolysis.
{ECO:0000256|HAMAP-Rule:MF_00464}.
MOD_RES 63 63 Pyruvic acid (Ser); by autocatalysis.
{ECO:0000256|HAMAP-Rule:MF_00464}.
SEQUENCE 431 AA; 48129 MW; 8C37C35F45874790 CRC64;
MKSLGRHILV EFHGCSAEIL NDVPRIEHDM LEAATRSGAT IINSVFHHFS PFGVSGVIVI
QESHLAIHTW PEYRYAAVDL FTCGDSVNPW VSYESLKTAF EAEHGSAIEL NRGQLELLEK
INIDLGDMRD QATQKLMPPK QSRSVWFTDK DDNIALSIRH KGDRLFQEKS PYQLVEIYDT
FKYGKMLTVD KMVMCSEKDE TAYHEMIIHV PMLAHATATP GLKKALVIGG GDGGSVREIL
RHPQVESVTM VEIDEVVVRA SRKFLPSLSS SLDDPKLNLI IGDGINYLED AQDESFDFIV
VDSSDPVGPS VGLFSAEFYK NVHRVLTPHG VIAAQSESPR FNQAAFVDLT GCLQNIFGPE
NIHTYLAFIQ TYPTGMWSFT YGTKNGIHPV DALDPAGATE FTKKHDLQYY NPDVHRAAFC
LPTFIQNLLA R


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