ID A0A365U8J2_9RHOB Unreviewed; 176 AA.
AC A0A365U8J2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=S-adenosylmethionine decarboxylase proenzyme {ECO:0000256|HAMAP-Rule:MF_00464};
DE Short=AdoMetDC {ECO:0000256|HAMAP-Rule:MF_00464};
DE Short=SAMDC {ECO:0000256|HAMAP-Rule:MF_00464};
DE EC=4.1.1.50 {ECO:0000256|HAMAP-Rule:MF_00464};
DE Contains:
DE RecName: Full=S-adenosylmethionine decarboxylase beta chain {ECO:0000256|HAMAP-Rule:MF_00464};
DE Contains:
DE RecName: Full=S-adenosylmethionine decarboxylase alpha chain {ECO:0000256|HAMAP-Rule:MF_00464};
GN Name=speD {ECO:0000313|EMBL:RBI85065.1};
GN Synonyms=speH {ECO:0000256|HAMAP-Rule:MF_00464};
GN ORFNames=DRV85_10410 {ECO:0000313|EMBL:RBI85065.1};
OS Rhodosalinus halophilus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodosalinus.
OX NCBI_TaxID=2259333 {ECO:0000313|EMBL:RBI85065.1, ECO:0000313|Proteomes:UP000253370};
RN [1] {ECO:0000313|EMBL:RBI85065.1, ECO:0000313|Proteomes:UP000253370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E84 {ECO:0000313|EMBL:RBI85065.1,
RC ECO:0000313|Proteomes:UP000253370};
RA Liu Z.-W., Lu D.-C.;
RT "Rhodosalinus sp. strain E84T genomic sequence and assembly.";
RL Submitted (JUL-2018) 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_00464}.
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_00464};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00464};
CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00464};
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_00464}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged as a
CC dimer of alpha/beta heterodimers. {ECO:0000256|HAMAP-Rule:MF_00464}.
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_00464}.
CC -!- SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 1
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00464}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RBI85065.1}.
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DR EMBL; QNTQ01000008; RBI85065.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A365U8J2; -.
DR OrthoDB; 9793120at2; -.
DR UniPathway; UPA00331; UER00451.
DR Proteomes; UP000253370; 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_00464; AdoMetDC_1; 1.
DR InterPro; IPR003826; AdoMetDC_fam_prok.
DR InterPro; IPR016067; S-AdoMet_deCO2ase_core.
DR InterPro; IPR017716; S-AdoMet_deCOase_pro-enz.
DR NCBIfam; TIGR03330; SAM_DCase_Bsu; 1.
DR PANTHER; PTHR33866; S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME; 1.
DR PANTHER; PTHR33866:SF2; S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME; 1.
DR Pfam; PF02675; AdoMet_dc; 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_00464};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW Rule:MF_00464};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00464};
KW Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115, ECO:0000256|HAMAP-
KW Rule:MF_00464};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|HAMAP-Rule:MF_00464};
KW Reference proteome {ECO:0000313|Proteomes:UP000253370};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00464};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW Rule:MF_00464};
KW Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066, ECO:0000256|HAMAP-
KW Rule:MF_00464};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_00464}.
FT CHAIN 1..115
FT /note="S-adenosylmethionine decarboxylase beta chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT /id="PRO_5023241358"
FT CHAIN 116..176
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT /id="PRO_5023241357"
FT REGION 17..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 116
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT ACT_SITE 121
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT ACT_SITE 136
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT SITE 115..116
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT MOD_RES 116
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
SQ SEQUENCE 176 AA; 19234 MW; 0A0B7C50BE61FFE2 CRC64;
MKDATLFQLG IGLETGAQEE DTARGTHAPR DTDTDTDARD IFDADRDDHF IRRDGAVFAG
THLIIEVVDG HGLDDEARIQ QAFRDCVDRC GATLLHIHTH KFSPQGVSGV AVLAESHISV
HTWPEIGYGA FDVFMCGDAQ PWRAVDVLRH AFSTADVRVK ELRRGEDVVA DAGIAA
//
