SPED_BREBN
ID SPED_BREBN Reviewed; 269 AA.
AC C0Z4Q5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=BBR47_08050;
OS Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=358681;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47 / JCM 6285 / NBRC 100599;
RA Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA Udaka S., Tanikawa S., Fujita N.;
RT "Brevibacillus brevis strain 47, complete genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; AP008955; BAH41782.1; -; Genomic_DNA.
DR RefSeq; WP_012684545.1; NC_012491.1.
DR AlphaFoldDB; C0Z4Q5; -.
DR SMR; C0Z4Q5; -.
DR STRING; 358681.BBR47_08050; -.
DR EnsemblBacteria; BAH41782; BAH41782; BBR47_08050.
DR KEGG; bbe:BBR47_08050; -.
DR eggNOG; COG1586; Bacteria.
DR HOGENOM; CLU_092007_0_0_9; -.
DR OMA; HVTVHTY; -.
DR OrthoDB; 757383at2; -.
DR UniPathway; UPA00331; UER00451.
DR Proteomes; UP000001877; 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; Reference proteome; S-adenosyl-L-methionine; Schiff base;
KW Spermidine biosynthesis; Zymogen.
FT CHAIN 1..117
FT /note="S-adenosylmethionine decarboxylase beta chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00465"
FT /id="PRO_1000193158"
FT CHAIN 118..269
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00465"
FT /id="PRO_1000193159"
FT ACT_SITE 118
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00465"
FT ACT_SITE 123
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00465"
FT ACT_SITE 146
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00465"
FT SITE 117..118
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00465"
FT MOD_RES 118
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00465"
SQ SEQUENCE 269 AA; 31337 MW; FAC383B78CBF7EE5 CRC64;
MEQKTEHNVT LHGFNNLTKS LSFNMYDICY TKTKEEREAY IEYIDEQYNA ERLTSILKNV
SDIIGAHVLN VAKQDYVPQG ASVTFLVSEG PVVEVPTESY EESPGPLPEN VVLQLDKSHI
TVHTYPEYHP TEGISTFRAD IDVSTCGEIS PLKALNYLIR SFDTDLMTID YKVRGFTRDI
HGYKLFIDHD ISSIQNYIPE EIKELFHMID VNVYQDNIFH TKCKRREFDL NNYLFGYTKD
RLTPEEQEDI TKQLQIEMDE IYYGKNFVN
