(data stored in ACNUC7421 zone)

SWISSPROT: SPED_PSEHT

ID   SPED_PSEHT              Reviewed;         270 AA.
AC   Q3IFT4;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 74.
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};
GN   OrderedLocusNames=PSHAa0199;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Catalyzes the decarboxylation of S-adenosylmethionine to
CC       S-adenosylmethioninamine (dcAdoMet), the propylamine donor
CC       required for the synthesis of the polyamines spermine and
CC       spermidine from the diamine putrescine. {ECO:0000255|HAMAP-
CC       Rule:MF_00465}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = S-adenosyl 3-
CC       (methylthio)propylamine + CO(2). {ECO:0000255|HAMAP-
CC       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.
CC       {ECO:0000255|HAMAP-Rule:MF_00465};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; S-
CC       adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from
CC       S-adenosyl-L-methionine: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_00465}.
CC   -!- SUBUNIT: Heterooctamer of four alpha and four beta chains arranged
CC       as a tetramer of alpha/beta heterodimers. {ECO:0000255|HAMAP-
CC       Rule:MF_00465}.
CC   -!- PTM: Is synthesized initially as an inactive proenzyme. Formation
CC       of the active enzyme involves a self-maturation process in which
CC       the active site pyruvoyl group is generated from an internal
CC       serine residue via an autocatalytic post-translational
CC       modification. Two non-identical subunits are generated from the
CC       proenzyme in this reaction, and the pyruvate is formed at the N-
CC       terminus of the alpha chain, which is derived from the carboxyl
CC       end of the proenzyme. The post-translation cleavage follows an
CC       unusual pathway, termed non-hydrolytic serinolysis, in which the
CC       side chain hydroxyl group of the serine supplies its oxygen atom
CC       to form the C-terminus of the beta chain, while the remainder of
CC       the serine residue undergoes an oxidative deamination to produce
CC       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}.
DR   EMBL; CR954246; CAI85302.1; -; Genomic_DNA.
DR   RefSeq; WP_011326917.1; NC_007481.1.
DR   ProteinModelPortal; Q3IFT4; -.
DR   STRING; 326442.PSHAa0199; -.
DR   EnsemblBacteria; CAI85302; CAI85302; PSHAa0199.
DR   GeneID; 32566608; -.
DR   KEGG; pha:PSHAa0199; -.
DR   eggNOG; ENOG4105FDS; Bacteria.
DR   eggNOG; COG1586; LUCA.
DR   HOGENOM; HOG000116821; -.
DR   KO; K01611; -.
DR   OMA; YNAERLT; -.
DR   OrthoDB; POG091H02FE; -.
DR   UniPathway; UPA00331; UER00451.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.90.10; -; 1.
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   Pfam; PF02675; AdoMet_dc; 1.
DR   PIRSF; PIRSF001356; SAM_decarboxylas; 1.
DR   SUPFAM; SSF56276; SSF56276; 2.
DR   TIGRFAMs; TIGR03331; SAM_DCase_Eco; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3IFT4.
DR   SWISS-2DPAGE; Q3IFT4.
KW   Autocatalytic cleavage; Complete proteome; Decarboxylase; Lyase;
KW   Polyamine biosynthesis; Pyruvate; Reference proteome;
KW   S-adenosyl-L-methionine; Schiff base; Spermidine biosynthesis;
KW   Zymogen.
FT   CHAIN         1    116       S-adenosylmethionine decarboxylase beta
FT                                chain. {ECO:0000255|HAMAP-Rule:MF_00465}.
FT                                /FTId=PRO_0000273599.
FT   CHAIN       117    270       S-adenosylmethionine decarboxylase alpha
FT                                chain. {ECO:0000255|HAMAP-Rule:MF_00465}.
FT                                /FTId=PRO_0000273600.
FT   ACT_SITE    117    117       Schiff-base intermediate with substrate;
FT                                via pyruvic acid. {ECO:0000255|HAMAP-
FT                                Rule:MF_00465}.
FT   ACT_SITE    122    122       Proton acceptor; for processing activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_00465}.
FT   ACT_SITE    145    145       Proton donor; for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_00465}.
FT   SITE        116    117       Cleavage (non-hydrolytic); by autolysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_00465}.
FT   MOD_RES     117    117       Pyruvic acid (Ser); by autocatalysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_00465}.
SQ   SEQUENCE   270 AA;  30980 MW;  28D35391984D1458 CRC64;
     MNKPFDKLKL HGFNNLTKSL SFSIYDICYA KTEQQRKEYI EYIDEQYSAD RLTDILGEVV
     DIIGANILNV ARQDYEPQGA SVTILVSEEP VEEQQNYDAD EAPGPLPDSV VAHLDKSHIC
     VHTYPEAHPD DGICTFRADI EVSTCGIISP LKALNFLIHS LESDVVTIDY RVRGFTRDIN
     GVKHYIDHAI SSIQNFMTED TKEAYQMMDV NVYQENLFHT KMMLKETDLN TYLFGLSTDD
     LSDEEEEEIR SKLTREMQEI FYGRNLPDLD
//

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