ID G3IVJ8_METTV Unreviewed; 268 AA.
AC G3IVJ8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=S-adenosylmethionine decarboxylase proenzyme {ECO:0000256|HAMAP-Rule:MF_00465};
DE Short=AdoMetDC {ECO:0000256|HAMAP-Rule:MF_00465};
DE Short=SAMDC {ECO:0000256|HAMAP-Rule:MF_00465};
DE EC=4.1.1.50 {ECO:0000256|HAMAP-Rule:MF_00465};
DE Contains:
DE RecName: Full=S-adenosylmethionine decarboxylase beta chain {ECO:0000256|HAMAP-Rule:MF_00465};
DE Contains:
DE RecName: Full=S-adenosylmethionine decarboxylase alpha chain {ECO:0000256|HAMAP-Rule:MF_00465};
GN Name=speD {ECO:0000256|HAMAP-Rule:MF_00465};
GN ORFNames=Mettu_1759 {ECO:0000313|EMBL:EGW22925.1};
OS Methylobacter tundripaludum (strain ATCC BAA-1195 / DSM 17260 / SV96).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylobacter.
OX NCBI_TaxID=697282 {ECO:0000313|EMBL:EGW22925.1, ECO:0000313|Proteomes:UP000004664};
RN [1] {ECO:0000313|EMBL:EGW22925.1, ECO:0000313|Proteomes:UP000004664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1195 / DSM 17260 / SV96
RC {ECO:0000313|Proteomes:UP000004664};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Held B.,
RA Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N.,
RA Ovchinnikova G., Pagani I., Klotz M.G., Dispirito A.A., Murrell J.C.,
RA Dunfield P., Kalyuzhnaya M.G., Svenning M., Trotsenko Y.A., Stein L.Y.,
RA Woyke T.;
RT "Genomic sequence of Methylobacter tundripaludum SV96.";
RL Submitted (JUN-2011) 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:0000256|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:0000256|HAMAP-Rule:MF_00465};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00465};
CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00465}.
CC -!- SUBUNIT: Heterooctamer of four alpha and four beta chains arranged as a
CC tetramer of alpha/beta heterodimers. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00465}.
CC -!- SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00465}.
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DR EMBL; JH109152; EGW22925.1; -; Genomic_DNA.
DR RefSeq; WP_006890937.1; NZ_JH109152.1.
DR AlphaFoldDB; G3IVJ8; -.
DR STRING; 697282.Mettu_1759; -.
DR eggNOG; COG1586; Bacteria.
DR HOGENOM; CLU_092007_0_0_6; -.
DR OrthoDB; 5290709at2; -.
DR UniPathway; UPA00331; UER00451.
DR Proteomes; UP000004664; Unassembled WGS sequence.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.60.90.10; S-adenosylmethionine decarboxylase; 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 NCBIfam; TIGR03331; SAM_DCase_Eco; 1.
DR PANTHER; PTHR33866; S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME; 1.
DR PANTHER; PTHR33866:SF1; S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME; 1.
DR Pfam; PF02675; AdoMet_dc; 1.
DR PIRSF; PIRSF001356; SAM_decarboxylas; 1.
DR SUPFAM; SSF56276; S-adenosylmethionine decarboxylase; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813, ECO:0000256|HAMAP-
KW Rule:MF_00465};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW Rule:MF_00465};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00465};
KW Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115, ECO:0000256|HAMAP-
KW Rule:MF_00465};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|HAMAP-Rule:MF_00465};
KW Reference proteome {ECO:0000313|Proteomes:UP000004664};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_00465};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW Rule:MF_00465};
KW Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066, ECO:0000256|HAMAP-
KW Rule:MF_00465};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_00465}.
FT CHAIN 1..110
FT /note="S-adenosylmethionine decarboxylase beta chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00465"
FT /id="PRO_5023319488"
FT CHAIN 111..268
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00465"
FT /id="PRO_5023319489"
FT ACT_SITE 111
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00465"
FT ACT_SITE 116
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00465"
FT ACT_SITE 139
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00465"
FT SITE 110..111
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00465"
FT MOD_RES 111
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00465"
SQ SEQUENCE 268 AA; 30636 MW; AF85BCB9AFDC5260 CRC64;
MNKLQLHGFN NLTKSLSFNI YDICYAPAEQ QQAYIEYIDE AYNADKLTQI LKDVAEIIGA
QVLNIARQDY EPQGASVTML ISEGEAPPPP SMNSQSPGPL PETVLAHLDK SHITVHTYPE
SHPDNGISTF RADIDVSTCG RISPLKALNY LIHSFESDVV TMDYKVRGFT RDISGKKHYI
DHKITSIQDY IAIDTQESYQ MIDVNVYQEN IFHTKMMLKE TELENYLFEK ECDLSADQKA
AIESKLHKEV TEIFYGHNYR QRYEEVKA
//
