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SPED_AZOVD
ID   SPED_AZOVD              Reviewed;         264 AA.
AC   C1DHY4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=S-adenosylmethionine decarboxylase proenzyme {ECO:0000255|HAMAP-Rule:MF_00465};
DE            Short=AdoMetDC {ECO:0000255|HAMAP-Rule:MF_00465};
DE            Short=SAMDC {ECO:0000255|HAMAP-Rule:MF_00465};
DE            EC=4.1.1.50 {ECO:0000255|HAMAP-Rule:MF_00465};
DE   Contains:
DE     RecName: Full=S-adenosylmethionine decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_00465};
DE   Contains:
DE     RecName: Full=S-adenosylmethionine decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_00465};
DE   Flags: Precursor;
GN   Name=speD {ECO:0000255|HAMAP-Rule:MF_00465}; OrderedLocusNames=Avin_46080;
OS   Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=322710;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ / ATCC BAA-1303;
RX   PubMed=19429624; DOI=10.1128/jb.00504-09;
RA   Setubal J.C., Dos Santos P., Goldman B.S., Ertesvaag H., Espin G.,
RA   Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA   Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA   Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA   Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA   Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA   Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA   Dean D.R., Dixon R., Wood D.;
RT   "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT   to support diverse anaerobic metabolic processes.";
RL   J. Bacteriol. 191:4534-4545(2009).
CC   -!- FUNCTION: Catalyzes the decarboxylation of S-adenosylmethionine to S-
CC       adenosylmethioninamine (dcAdoMet), the propylamine donor required for
CC       the synthesis of the polyamines spermine and spermidine from the
CC       diamine putrescine. {ECO:0000255|HAMAP-Rule:MF_00465}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-
CC         (methylsulfanyl)propylamine; Xref=Rhea:RHEA:15981, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57443, ChEBI:CHEBI:59789; EC=4.1.1.50;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00465};
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00465};
CC       Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00465};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; S-adenosylmethioninamine
CC       biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine:
CC       step 1/1. {ECO:0000255|HAMAP-Rule:MF_00465}.
CC   -!- SUBUNIT: Heterooctamer of four alpha and four beta chains arranged as a
CC       tetramer of alpha/beta heterodimers. {ECO:0000255|HAMAP-Rule:MF_00465}.
CC   -!- PTM: Is synthesized initially as an inactive proenzyme. Formation of
CC       the active enzyme involves a self-maturation process in which the
CC       active site pyruvoyl group is generated from an internal serine residue
CC       via an autocatalytic post-translational modification. Two non-identical
CC       subunits are generated from the proenzyme in this reaction, and the
CC       pyruvate is formed at the N-terminus of the alpha chain, which is
CC       derived from the carboxyl end of the proenzyme. The post-translation
CC       cleavage follows an unusual pathway, termed non-hydrolytic serinolysis,
CC       in which the side chain hydroxyl group of the serine supplies its
CC       oxygen atom to form the C-terminus of the beta chain, while the
CC       remainder of the serine residue undergoes an oxidative deamination to
CC       produce ammonia and the pyruvoyl group blocking the N-terminus of the
CC       alpha chain. {ECO:0000255|HAMAP-Rule:MF_00465}.
CC   -!- SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00465}.
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DR   EMBL; CP001157; ACO80717.1; -; Genomic_DNA.
DR   RefSeq; WP_012703080.1; NC_012560.1.
DR   AlphaFoldDB; C1DHY4; -.
DR   STRING; 322710.Avin_46080; -.
DR   PRIDE; C1DHY4; -.
DR   EnsemblBacteria; ACO80717; ACO80717; Avin_46080.
DR   KEGG; avn:Avin_46080; -.
DR   eggNOG; COG1586; Bacteria.
DR   HOGENOM; CLU_092007_0_0_6; -.
DR   OMA; HVTVHTY; -.
DR   OrthoDB; 757383at2; -.
DR   UniPathway; UPA00331; UER00451.
DR   Proteomes; UP000002424; Chromosome.
DR   GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00465; AdoMetDC_2; 1.
DR   InterPro; IPR003826; AdoMetDC_fam_prok.
DR   InterPro; IPR009165; S-AdoMet_deCO2ase_bac.
DR   InterPro; IPR016067; S-AdoMet_deCO2ase_core.
DR   PANTHER; PTHR33866; PTHR33866; 1.
DR   Pfam; PF02675; AdoMet_dc; 1.
DR   PIRSF; PIRSF001356; SAM_decarboxylas; 1.
DR   SUPFAM; SSF56276; SSF56276; 1.
DR   TIGRFAMs; TIGR03331; SAM_DCase_Eco; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; Decarboxylase; Lyase; Polyamine biosynthesis;
KW   Pyruvate; S-adenosyl-L-methionine; Schiff base; Spermidine biosynthesis;
KW   Zymogen.
FT   CHAIN           1..112
FT                   /note="S-adenosylmethionine decarboxylase beta chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00465"
FT                   /id="PRO_1000206322"
FT   CHAIN           113..264
FT                   /note="S-adenosylmethionine decarboxylase alpha chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00465"
FT                   /id="PRO_1000206323"
FT   ACT_SITE        113
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00465"
FT   ACT_SITE        118
FT                   /note="Proton acceptor; for processing activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00465"
FT   ACT_SITE        141
FT                   /note="Proton donor; for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00465"
FT   SITE            112..113
FT                   /note="Cleavage (non-hydrolytic); by autolysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00465"
FT   MOD_RES         113
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00465"
SQ   SEQUENCE   264 AA;  30483 MW;  752DD839F549D38E CRC64;
     MKSKLKLHGF NNLTKTLSFN IYDICYAETP EDQQAYVRYI DEEYDAQRLT QILTDVVDII
     GANVLNIARQ DYDPQGASVT ILISEQPVEP TESQIEESPG PLPETILAHL DKSHITVHTY
     PEIHPVDGLA TFRVDIDVST CGVISPLKAL NYLIHQFDSD IVTVDYRVRG FTRDVEGRKH
     FIDHEINSIQ KYLSADTRAA YQMTDVNVYQ ENMFHTKMLL KDFDLDNYLF GDATLNLSVE
     QRKQVEKRLR HEMLEIFYAR NMPH
 
 
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