SPED_XANAC
ID SPED_XANAC Reviewed; 264 AA.
AC Q8PQ44;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 110.
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=XAC0484;
OS Xanthomonas axonopodis pv. citri (strain 306).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190486;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=306;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
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; AE008923; AAM35375.1; -; Genomic_DNA.
DR RefSeq; WP_007967854.1; NC_003919.1.
DR AlphaFoldDB; Q8PQ44; -.
DR SMR; Q8PQ44; -.
DR STRING; 190486.XAC0484; -.
DR EnsemblBacteria; AAM35375; AAM35375; XAC0484.
DR GeneID; 63989763; -.
DR GeneID; 66909690; -.
DR KEGG; xac:XAC0484; -.
DR eggNOG; COG1586; Bacteria.
DR HOGENOM; CLU_092007_0_0_6; -.
DR OMA; HVTVHTY; -.
DR UniPathway; UPA00331; UER00451.
DR Proteomes; UP000000576; 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_0000030065"
FT CHAIN 113..264
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00465"
FT /id="PRO_0000030066"
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; 30806 MW; 68B09FCB5F1C3EAB CRC64;
MVKPLPRLRL QGFNNLTKAL SFNIYDVCYA RTEEERQRYI EYIDEQYDAD RLTQILTDVA
EIIGANILNI ARQDYDPQGA SVTILISEEP VIDKKQAGKE LISDAVVAHM DKSHITVHTY
PETHPQEGIA TFRADIDVAT CGVISPLKAL NYLIESLESD IVIMDYRVRG FTRDVKGKKH
YIDHKINSIQ QFLAKNVKSR YEMFDVNVYQ ENIFHTKMHL KDFDLDQYLF EERAKNLSFK
ERMKIETLLK REIEELFHGR NLSE
