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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]

 A0A1Z3HL89_9CYAN        Unreviewed;       427 AA.
A0A1Z3HL89;
27-SEP-2017, integrated into UniProtKB/TrEMBL.
27-SEP-2017, sequence version 1.
20-JUN-2018, entry version 10.
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_1 {ECO:0000313|EMBL:ASC70857.1};
Synonyms=speE {ECO:0000256|HAMAP-Rule:MF_00198},
speH {ECO:0000256|HAMAP-Rule:MF_00464};
ORFNames=XM38_018040 {ECO:0000313|EMBL:ASC70857.1};
Halomicronema hongdechloris C2206.
Bacteria; Cyanobacteria; Synechococcales; Leptolyngbyaceae;
Halomicronema.
NCBI_TaxID=1641165 {ECO:0000313|EMBL:ASC70857.1, ECO:0000313|Proteomes:UP000191901};
[1] {ECO:0000313|EMBL:ASC70857.1, ECO:0000313|Proteomes:UP000191901}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C2206 {ECO:0000313|EMBL:ASC70857.1,
ECO:0000313|Proteomes:UP000191901};
PubMed=26514405; DOI=.1016/j.bbabio.2015.10.009;
Li Y., Lin Y., Garvey C.J., Birch D., Corkery R.W., Loughlin P.C.,
Scheer H., Willows R.D., Chen M.;
"Characterization of red-shifted phycobilisomes isolated from the
chlorophyll f-containing cyanobacterium Halomicronema hongdechloris.";
Biochim. Biophys. Acta 1857:107-114(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, ECO:0000256|RuleBase:RU003837}.
-!- 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}.
-!- 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}.
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EMBL; CP021983; ASC70857.1; -; Genomic_DNA.
KEGG; hhg:XM38_018040; -.
KO; K00797; -.
UniPathway; UPA00248; UER00314.
UniPathway; UPA00331; UER00451.
Proteomes; UP000191901; Chromosome.
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.
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:UP000191901};
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_00464,
ECO:0000256|PROSITE-ProRule:PRU00354};
Pyruvate {ECO:0000256|HAMAP-Rule:MF_00464};
Reference proteome {ECO:0000313|Proteomes:UP000191901};
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_00464,
ECO:0000256|RuleBase:RU003837};
Transferase {ECO:0000256|HAMAP-Rule:MF_00198, ECO:0000256|PROSITE-
ProRule:PRU00354, ECO:0000256|RuleBase:RU003836,
ECO:0000313|EMBL:ASC70857.1};
Zymogen {ECO:0000256|HAMAP-Rule:MF_00464}.
DOMAIN 144 380 PABS. {ECO:0000259|PROSITE:PS51006}.
REGION 279 280 S-adenosylmethioninamine binding.
{ECO:0000256|HAMAP-Rule:MF_00198}.
REGION 299 301 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 298 298 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 228 228 Polyamine. {ECO:0000256|HAMAP-
Rule:MF_00198}.
BINDING 248 248 S-adenosylmethioninamine.
{ECO:0000256|HAMAP-Rule:MF_00198}.
BINDING 305 305 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 427 AA; 47829 MW; CA7BEAD4C58E3B13 CRC64;
MHSLGRHILV EFFGCSSEIL NDVPYIENSM RRAAQEAGAT LISSVFHHFS PFGVSGVVVI
QESHLAIHTW PEYRYAAVDL FTCGHAVNPW VSYNILKQAF QADHGSAIEL NRGALELLEK
SEVDLGELRD QVTQKLVEPK FSRSVWFTDR DENIALSIRH KGDRVFREKS PYQTVEIFDT
YAYGKMLTVD NVVMCTEKDE NAYHEMIVHV PMLLNPDIRR VLVIGGGDGG SVREILRHPQ
VEAVTMVEID EVVVRASRQY LPSLSHALDD PKLNLIIGDG IRFMQAAASE AYDLIVIDSS
DPVGPSEGLF SPSFYEQAHR CLKPGGVMTA QSESPRFNHA AFVDLVQCLR SIFGRDYVHC
YLAFIPTYPT GMWSFTYSSK GGADPIRGFD RKRAAAFAAQ ENLQYYNADI HPAAFCLPTF
VKNMLNG


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