SPED_NITOC
ID SPED_NITOC Reviewed; 276 AA.
AC Q3JCI4;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=Noc_0951;
OS Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB
OS 11848 / C-107).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Nitrosococcus.
OX NCBI_TaxID=323261;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB 11848 / C-107;
RX PubMed=16957257; DOI=10.1128/aem.00463-06;
RA Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J.,
RA Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T.,
RA Vergez L.M., Ward B.B.;
RT "Complete genome sequence of the marine, chemolithoautotrophic, ammonia-
RT oxidizing bacterium Nitrosococcus oceani ATCC 19707.";
RL Appl. Environ. Microbiol. 72:6299-6315(2006).
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; CP000127; ABA57462.1; -; Genomic_DNA.
DR RefSeq; WP_002811356.1; NC_007484.1.
DR AlphaFoldDB; Q3JCI4; -.
DR SMR; Q3JCI4; -.
DR STRING; 323261.Noc_0951; -.
DR EnsemblBacteria; ABA57462; ABA57462; Noc_0951.
DR KEGG; noc:Noc_0951; -.
DR eggNOG; COG1586; Bacteria.
DR HOGENOM; CLU_092007_0_0_6; -.
DR OMA; HVTVHTY; -.
DR OrthoDB; 757383at2; -.
DR UniPathway; UPA00331; UER00451.
DR Proteomes; UP000006838; 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..116
FT /note="S-adenosylmethionine decarboxylase beta chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00465"
FT /id="PRO_0000364395"
FT CHAIN 117..276
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00465"
FT /id="PRO_0000364396"
FT ACT_SITE 117
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00465"
FT ACT_SITE 122
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00465"
FT ACT_SITE 145
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00465"
FT SITE 116..117
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00465"
FT MOD_RES 117
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00465"
SQ SEQUENCE 276 AA; 31858 MW; 87797C4CB268D0F6 CRC64;
MTRAFNKIKL HGFNNLTKTL SFNVYDICYA QTFQQRREYI EYIDEEYNAE RLTHILTEVA
EIIGANILNV ARQNYEPQGA SVTMLIAEDE TEIHQQFTNA EEPGPLPESL VCHLDKSHLT
VHTYPESHPE NGISTFRADI DVSTCGRVSP LRALNYLIHS LESDIVTMDY RVRGFTRNVY
GGKHFIDHAI NSIQNFIAED TKGRYHMIDV NIYQENIFHT KMMLKDFELD DYLFGGNACD
LASQEQQAIA DRVKNEMLEI FYGKNIPHPD IESSRR
