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S-adenosylmethionine decarboxylase proenzyme (AdoMetDC) (SAMDC) (EC 4.1.1.50) [Cleaved into: S-adenosylmethionine decarboxylase alpha chain; S-adenosylmethionine decarboxylase beta chain]

 Q1PK83_PROMR            Unreviewed;       144 AA.
Q1PK83;
16-MAY-2006, integrated into UniProtKB/TrEMBL.
16-MAY-2006, sequence version 1.
22-NOV-2017, entry version 53.
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=speH {ECO:0000256|HAMAP-Rule:MF_00464};
ORFNames=HF10-11H11_0026 {ECO:0000313|EMBL:ABE11143.1};
uncultured Prochlorococcus marinus clone HF10-11H11.
Bacteria; Cyanobacteria; Synechococcales; Prochloraceae;
Prochlorococcus.
NCBI_TaxID=379375 {ECO:0000313|EMBL:ABE11143.1};
[1] {ECO:0000313|EMBL:ABE11143.1}
NUCLEOTIDE SEQUENCE.
PubMed=16556843; DOI=10.1126/science.1122050;
Coleman M.L., Sullivan M.B., Martiny A.C., Steglich C., Barry K.,
Delong E.F., Chisholm S.W.;
"Genomic islands and the ecology and evolution of Prochlorococcus.";
Science 311:1768-1770(2006).
[2] {ECO:0000313|EMBL:ABE11143.1}
NUCLEOTIDE SEQUENCE.
US DOE Joint Genome Institute (JGI);
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
Hammon N., Israni S., Richardson P.;
"Sequencing of the draft fosmids and assembly of Prochlorococcus
marinus environmental genome fragment.";
Submitted (APR-2006) 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:SAAS00948089}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = S-adenosyl 3-
(methylthio)propylamine + CO(2). {ECO:0000256|HAMAP-Rule:MF_00464,
ECO:0000256|SAAS:SAAS00948090}.
-!- 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:SAAS00948084}.
-!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged
as a dimer of alpha/beta heterodimers. {ECO:0000256|HAMAP-
Rule:MF_00464}.
-!- 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}.
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EMBL; DQ366723; ABE11143.1; -; Genomic_DNA.
ProteinModelPortal; Q1PK83; -.
UniPathway; UPA00331; UER00451.
GO; GO:0004014; F:adenosylmethionine decarboxylase 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.
InterPro; IPR003826; AdoMetDC_fam_prok.
InterPro; IPR016067; S-AdoMet_deCO2ase_core.
InterPro; IPR017716; S-AdoMet_deCOase_pro-enz.
PANTHER; PTHR33866; PTHR33866; 1.
Pfam; PF02675; AdoMet_dc; 1.
SUPFAM; SSF56276; SSF56276; 1.
TIGRFAMs; TIGR03330; SAM_DCase_Bsu; 1.
3: Inferred from homology;
Autocatalytic cleavage {ECO:0000256|HAMAP-Rule:MF_00464};
Decarboxylase {ECO:0000256|HAMAP-Rule:MF_00464};
Lyase {ECO:0000256|HAMAP-Rule:MF_00464};
Polyamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00464};
Pyruvate {ECO:0000256|HAMAP-Rule:MF_00464};
S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00464,
ECO:0000256|SAAS:SAAS00948082};
Schiff base {ECO:0000256|HAMAP-Rule:MF_00464};
Spermidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00464,
ECO:0000256|SAAS:SAAS00948091};
Zymogen {ECO:0000256|HAMAP-Rule:MF_00464}.
ACT_SITE 81 81 Schiff-base intermediate with substrate;
via pyruvic acid. {ECO:0000256|HAMAP-
Rule:MF_00464}.
ACT_SITE 86 86 Proton acceptor; for processing activity.
{ECO:0000256|HAMAP-Rule:MF_00464}.
ACT_SITE 101 101 Proton donor; for catalytic activity.
{ECO:0000256|HAMAP-Rule:MF_00464}.
SITE 80 81 Cleavage (non-hydrolytic); by autolysis.
{ECO:0000256|HAMAP-Rule:MF_00464}.
MOD_RES 81 81 Pyruvic acid (Ser); by autocatalysis.
{ECO:0000256|HAMAP-Rule:MF_00464}.
SEQUENCE 144 AA; 16464 MW; 481E6ED05D87C908 CRC64;
MEIYKKSHIL SSLSDEQKLS YQSKHLLLEL YRCDREKLND ECFLRCILNR AAKLANATVL
NLISNKFEPQ GVTVIALLAE SHISIHTWPE SNYSAVDIFT CGQKMMPELA SQYLIESLIA
KEHSLRVIER NPPSAVSKQI RTFV


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