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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]

 B3QRX7_CHLT3            Unreviewed;       438 AA.
B3QRX7;
02-SEP-2008, integrated into UniProtKB/TrEMBL.
02-SEP-2008, sequence version 1.
07-NOV-2018, entry version 81.
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 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};
OrderedLocusNames=Ctha_1471 {ECO:0000313|EMBL:ACF13930.1};
Chloroherpeton thalassium (strain ATCC 35110 / GB-78).
Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
Chloroherpeton.
NCBI_TaxID=517418 {ECO:0000313|EMBL:ACF13930.1, ECO:0000313|Proteomes:UP000001208};
[1] {ECO:0000313|EMBL:ACF13930.1, ECO:0000313|Proteomes:UP000001208}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 35110 / GB-78 {ECO:0000313|Proteomes:UP000001208};
US DOE Joint Genome Institute;
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F.,
Land M., Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T.,
Zhao F., Overmann J., Bryant D.A., Richardson P.;
"Complete sequence of Chloroherpeton thalassium ATCC 35110.";
Submitted (JUN-2008) 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: 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: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; CP001100; ACF13930.1; -; Genomic_DNA.
RefSeq; WP_012500014.1; NC_011026.1.
ProteinModelPortal; B3QRX7; -.
STRING; 517418.Ctha_1471; -.
EnsemblBacteria; ACF13930; ACF13930; Ctha_1471.
KEGG; cts:Ctha_1471; -.
eggNOG; ENOG4105CCX; Bacteria.
eggNOG; COG0421; LUCA.
eggNOG; COG1586; LUCA.
HOGENOM; HOG000256146; -.
KO; K00797; -.
OMA; CAIDFYH; -.
OrthoDB; POG091H029F; -.
BioCyc; CTHA517418:G1GC9-1537-MONOMER; -.
UniPathway; UPA00248; UER00314.
UniPathway; UPA00331; UER00451.
Proteomes; UP000001208; 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:UP000001208};
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};
Reference proteome {ECO:0000313|Proteomes:UP000001208};
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 147 383 PABS. {ECO:0000259|PROSITE:PS51006}.
REGION 282 283 S-adenosylmethioninamine binding.
{ECO:0000256|HAMAP-Rule:MF_00198}.
REGION 302 304 Polyamine binding. {ECO:0000256|HAMAP-
Rule:MF_00198}.
ACT_SITE 65 65 Schiff-base intermediate with substrate;
via pyruvic acid. {ECO:0000256|HAMAP-
Rule:MF_00464}.
ACT_SITE 70 70 Proton acceptor; for processing activity.
{ECO:0000256|HAMAP-Rule:MF_00464}.
ACT_SITE 85 85 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 152 152 Polyamine. {ECO:0000256|HAMAP-
Rule:MF_00198}.
BINDING 176 176 S-adenosylmethioninamine.
{ECO:0000256|HAMAP-Rule:MF_00198}.
BINDING 207 207 Polyamine. {ECO:0000256|HAMAP-
Rule:MF_00198}.
BINDING 231 231 Polyamine. {ECO:0000256|HAMAP-
Rule:MF_00198}.
BINDING 251 251 S-adenosylmethioninamine.
{ECO:0000256|HAMAP-Rule:MF_00198}.
BINDING 308 308 S-adenosylmethioninamine; via carbonyl
oxygen. {ECO:0000256|HAMAP-
Rule:MF_00198}.
SITE 64 65 Cleavage (non-hydrolytic); by autolysis.
{ECO:0000256|HAMAP-Rule:MF_00464}.
MOD_RES 65 65 Pyruvic acid (Ser); by autocatalysis.
{ECO:0000256|HAMAP-Rule:MF_00464}.
SEQUENCE 438 AA; 49954 MW; 6E2EE23A0098D6C5 CRC64;
MSGKSLGKHI LVEFYDCTPE VLDDVIHIER SMVKAAEIAN ATIINTGFHH FSPYGVSGVV
VIQESHLTIH TWPEYGYASV DIFSCGDTVD PWAAYTSLKE ALGAKSGSTM ELRRGQEKLL
NKQYNIPVFG EETPQREMQY SPQYARNIWF TEKGHNIALS LRHTGDLLYR KRSPYQRVEI
YDTFAYGKML TIDGLVMCTE KDEYVYHEMI SHVPMLTHPN PKRVLVIGGG DGGTIREILR
HESLEEVVMV EIDGAVVEAC REFLPAIASE FENPKLDLRI EDGVKYVMES PDKSFDIVIV
DSSDPVGPNE GLFTEEFYRN AYRILADDGI MVTQSESPRM NVRTFKELFH LYKKIFGMEN
VFCYLAFIPT YTSGMWSFSY STKCSAHPLK NLDRERAAEF SREQHLKYYN EGVHQGAFAL
PNFVVELLEE DITVEHTL


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