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Database: UniProt
Entry: A0A1H9BT50_9FIRM
LinkDB: A0A1H9BT50_9FIRM
Original site: A0A1H9BT50_9FIRM 
ID   A0A1H9BT50_9FIRM        Unreviewed;       265 AA.
AC   A0A1H9BT50;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=SAMN02910289_00903 {ECO:0000313|EMBL:SEP92136.1};
OS   Lachnospiraceae bacterium RM5.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1200721 {ECO:0000313|EMBL:SEP92136.1, ECO:0000313|Proteomes:UP000199252};
RN   [1] {ECO:0000313|EMBL:SEP92136.1, ECO:0000313|Proteomes:UP000199252}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM5 {ECO:0000313|EMBL:SEP92136.1,
RC   ECO:0000313|Proteomes:UP000199252};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOFK01000003; SEP92136.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9BT50; -.
DR   STRING; 1200721.SAMN02910289_00903; -.
DR   OrthoDB; 5290709at2; -.
DR   UniPathway; UPA00331; UER00451.
DR   Proteomes; UP000199252; 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:UP000199252};
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..112
FT                   /note="S-adenosylmethionine decarboxylase beta chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00465"
FT                   /id="PRO_5023293365"
FT   CHAIN           113..265
FT                   /note="S-adenosylmethionine decarboxylase alpha chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00465"
FT                   /id="PRO_5023293364"
FT   ACT_SITE        113
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00465"
FT   ACT_SITE        118
FT                   /note="Proton acceptor; for processing activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00465"
FT   ACT_SITE        141
FT                   /note="Proton donor; for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00465"
FT   SITE            112..113
FT                   /note="Cleavage (non-hydrolytic); by autolysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00465"
FT   MOD_RES         113
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00465"
SQ   SEQUENCE   265 AA;  30878 MW;  FD4302956AB9D631 CRC64;
     MNDKLKLYGF NNLTKSLSFN IYDVCYAKTE REQKEYIEYV DEQYNSDRLV KILCNVAEKI
     GAHVLNISKQ DYEPQGASVT ILMAEKHMYD TRESDVLNTS FKNDEILLHL DKSHITVHTY
     PEYHPENSIA TFRVDIDVAT CGEITPLSTL DYLIGSFDSD IITMDYKVRG FTRQIDGQKL
     FIDHKIKSIQ DFIDNETLKK YDAIDVNIYQ SNIFHTKMVI KDIELQNYLF NINADDLPLD
     KQFEIMNSLK REMAEIFSGT NIFLE
//
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