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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]

 A0A0P0CVW3_9BACT        Unreviewed;       427 AA.
A0A0P0CVW3;
20-JAN-2016, integrated into UniProtKB/TrEMBL.
20-JAN-2016, sequence version 1.
16-JAN-2019, entry version 32.
RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00198, ECO:0000256|HAMAP-Rule:MF_00464};
Includes:
RecName: Full=Polyamine aminopropyltransferase {ECO:0000256|HAMAP-Rule:MF_00198};
AltName: Full=Putrescine aminopropyltransferase {ECO:0000256|HAMAP-Rule:MF_00198};
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};
Includes:
RecName: Full=S-adenosylmethionine decarboxylase proenzyme {ECO:0000256|HAMAP-Rule:MF_00464};
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};
Contains:
RecName: Full=S-adenosylmethionine decarboxylase beta chain {ECO:0000256|HAMAP-Rule:MF_00464};
Contains:
RecName: Full=S-adenosylmethionine decarboxylase alpha chain {ECO:0000256|HAMAP-Rule:MF_00464};
Name=speE {ECO:0000256|HAMAP-Rule:MF_00198};
Synonyms=speH {ECO:0000256|HAMAP-Rule:MF_00464};
ORFNames=DC20_19995 {ECO:0000313|EMBL:ALJ00854.1};
Rufibacter tibetensis.
Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Hymenobacteraceae;
Rufibacter.
NCBI_TaxID=512763 {ECO:0000313|EMBL:ALJ00854.1, ECO:0000313|Proteomes:UP000061382};
[1] {ECO:0000313|EMBL:ALJ00854.1, ECO:0000313|Proteomes:UP000061382}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=1351 {ECO:0000313|EMBL:ALJ00854.1,
ECO:0000313|Proteomes:UP000061382};
Dai J.;
"Complete genome sequence of Rufibacter tibetensis strain 1351t, a
radiation-resistant bacterium from tibet plateau.";
Submitted (AUG-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}.
-!- 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:
Reaction=H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-
(methylsulfanyl)propylamine; Xref=Rhea:RHEA:15981,
ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57443,
ChEBI:CHEBI:59789; EC=4.1.1.50; Evidence={ECO:0000256|HAMAP-
Rule:MF_00464};
-!- CATALYTIC ACTIVITY:
Reaction=putrescine + S-adenosyl 3-(methylsulfanyl)propylamine =
H(+) + S-methyl-5'-thioadenosine + spermidine;
Xref=Rhea:RHEA:12721, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509,
ChEBI:CHEBI:57443, ChEBI:CHEBI:57834, ChEBI:CHEBI:326268;
EC=2.5.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00198,
ECO:0000256|RuleBase:RU003837};
-!- 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:SAAS01095326}.
-!- 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; CP012643; ALJ00854.1; -; Genomic_DNA.
RefSeq; WP_062545467.1; NZ_CP012643.1.
EnsemblBacteria; ALJ00854; ALJ00854; DC20_19995.
KEGG; rti:DC20_19995; -.
PATRIC; fig|512763.3.peg.4392; -.
KO; K00797; -.
OrthoDB; 1613081at2; -.
UniPathway; UPA00248; UER00314.
UniPathway; UPA00331; UER00451.
Proteomes; UP000061382; 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:UP000061382};
Cytoplasm {ECO:0000256|SAAS:SAAS01095314};
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,
ECO:0000256|RuleBase:RU003837};
Transferase {ECO:0000256|HAMAP-Rule:MF_00198, ECO:0000256|PROSITE-
ProRule:PRU00354, ECO:0000256|RuleBase:RU003836};
Zymogen {ECO:0000256|HAMAP-Rule:MF_00464}.
DOMAIN 143 379 PABS. {ECO:0000259|PROSITE:PS51006}.
REGION 278 279 S-adenosylmethioninamine binding.
{ECO:0000256|HAMAP-Rule:MF_00198}.
REGION 298 300 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 297 297 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 203 203 Polyamine. {ECO:0000256|HAMAP-
Rule:MF_00198}.
BINDING 227 227 Polyamine. {ECO:0000256|HAMAP-
Rule:MF_00198}.
BINDING 247 247 S-adenosylmethioninamine.
{ECO:0000256|HAMAP-Rule:MF_00198}.
BINDING 304 304 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; 47480 MW; 072E4F4207F12671 CRC64;
MDALGRHILV EFYNCSPELM NDVVHIENSM VAAAETAGAT VINSTFHHFS PYGVSGVVVI
QESHLAIHTW PEYGYAAVDL FTCGDSVDPW VSYNYLIEAF KASHGSSMEC LRGQQRLLNR
TDFTVEARDS GQQIAPIPKI TRDVWFTERD ENIALSLKHT GTQLYKKQSP YQKVEVFETL
AYGNMLTLDG MVMCTQKDEY VYHEMITHVP VFSHGNVKRA LVIGGGDGGT VRELLRHDCI
EEVVLVEIDE LVIEACKAHL PETASAFGNP KLKLLVEDGI KYIQECADSA FDLIIVDSAD
PVGPGEGLFT VEFYTQVHRC LTAEGVMITQ SESPRFNTNV FVEIFDTYKG IFGQNNVHCY
LAAIPTYPTG TWSFSFSSKG SVHPKKFNLE TAAAFSQAQG LRYYNEDIHV AAFALPNFVK
ELLSSKA


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