(data stored in ACNUC7421 zone)

SWISSPROT: SPED_ECO57

ID   SPED_ECO57              Reviewed;         264 AA.
AC   P0A7F7; P09159;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   05-JUL-2017, entry version 76.
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=Z0130, ECs0124;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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; AE005174; AAG54424.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33547.1; -; Genomic_DNA.
DR   PIR; D85495; D85495.
DR   PIR; D90644; D90644.
DR   RefSeq; NP_308151.1; NC_002695.1.
DR   RefSeq; WP_000734287.1; NZ_MWVM01000012.1.
DR   ProteinModelPortal; P0A7F7; -.
DR   STRING; 155864.Z0130; -.
DR   EnsemblBacteria; AAG54424; AAG54424; Z0130.
DR   EnsemblBacteria; BAB33547; BAB33547; BAB33547.
DR   GeneID; 913693; -.
DR   KEGG; ece:Z0130; -.
DR   KEGG; ecs:ECs0124; -.
DR   PATRIC; fig|386585.9.peg.222; -.
DR   eggNOG; ENOG4105FDS; Bacteria.
DR   eggNOG; COG1586; LUCA.
DR   HOGENOM; HOG000116821; -.
DR   KO; K01611; -.
DR   UniPathway; UPA00331; UER00451.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
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; P0A7F7.
DR   SWISS-2DPAGE; P0A7F7.
KW   Autocatalytic cleavage; Complete proteome; Decarboxylase; Lyase;
KW   Polyamine biosynthesis; Pyruvate; S-adenosyl-L-methionine;
KW   Schiff base; Spermidine biosynthesis; Zymogen.
FT   CHAIN         1    111       S-adenosylmethionine decarboxylase beta
FT                                chain. {ECO:0000255|HAMAP-Rule:MF_00465}.
FT                                /FTId=PRO_0000030045.
FT   CHAIN       112    264       S-adenosylmethionine decarboxylase alpha
FT                                chain. {ECO:0000255|HAMAP-Rule:MF_00465}.
FT                                /FTId=PRO_0000030046.
FT   ACT_SITE    112    112       Schiff-base intermediate with substrate;
FT                                via pyruvic acid. {ECO:0000255|HAMAP-
FT                                Rule:MF_00465}.
FT   ACT_SITE    117    117       Proton acceptor; for processing activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_00465}.
FT   ACT_SITE    140    140       Proton donor; for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_00465}.
FT   SITE        111    112       Cleavage (non-hydrolytic); by autolysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_00465}.
FT   MOD_RES     112    112       Pyruvic acid (Ser); by autocatalysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_00465}.
SQ   SEQUENCE   264 AA;  30385 MW;  E228BCF8EBDD0325 CRC64;
     MKKLKLHGFN NLTKSLSFCI YDICYAKTAE ERDGYIAYID ELYNANRLTE ILSETCSIIG
     ANILNIARQD YEPQGASVTI LVSEEPVDPK LIDKTEHPGP LPETVVAHLD KSHICVHTYP
     ESHPEGGLCT FRADIEVSTC GVISPLKALN YLIHQLESDI VTIDYRVRGF TRDINGMKHF
     IDHEINSIQN FMSDDMKALY DMVDVNVYQE NIFHTKMLLK EFDLKHYMFH TKPEDLTDSE
     RQEITAALWK EMREIYYGRN MPAV
//

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