ID C8WR51_ALIAD Unreviewed; 127 AA.
AC C8WR51;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 81.
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=speH {ECO:0000256|HAMAP-Rule:MF_00464};
GN OrderedLocusNames=Aaci_2211 {ECO:0000313|EMBL:ACV59220.1};
OS Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 /
OS DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC 15652 / NCIMB 11725 /
OS NRRL B-14509 / 104-IA) (Bacillus acidocaldarius).
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=521098 {ECO:0000313|EMBL:ACV59220.1, ECO:0000313|Proteomes:UP000001917};
RN [1] {ECO:0000313|Proteomes:UP000001917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27009 / DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC
RC 15652 / NCIMB 11725 / NRRL B-14509 / 104-IA
RC {ECO:0000313|Proteomes:UP000001917};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Ovchinnikova G., Chertkov O., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Pukall R., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of Alicyclobacillus acidocaldarius subsp.
RT acidocaldarius DSM 446.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACV59220.1, ECO:0000313|Proteomes:UP000001917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27009 / DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC
RC 15652 / NCIMB 11725 / NRRL B-14509 / 104-IA
RC {ECO:0000313|Proteomes:UP000001917};
RX PubMed=21304673; DOI=10.4056/sigs.591104;
RA Mavromatis K., Sikorski J., Lapidus A., Glavina Del Rio T., Copeland A.,
RA Tice H., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L.,
RA Pitluck S., Ivanova N., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Meincke L.,
RA Sims D., Chertkov O., Han C., Brettin T., Detter J.C., Wahrenburg C.,
RA Rohde M., Pukall R., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Alicyclobacillus acidocaldarius type strain
RT (104-IA).";
RL Stand. Genomic Sci. 2:9-18(2010).
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}.
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DR EMBL; CP001727; ACV59220.1; -; Genomic_DNA.
DR RefSeq; WP_008340238.1; NC_013205.1.
DR AlphaFoldDB; C8WR51; -.
DR STRING; 521098.Aaci_2211; -.
DR KEGG; aac:Aaci_2211; -.
DR eggNOG; COG1586; Bacteria.
DR HOGENOM; CLU_125470_2_3_9; -.
DR UniPathway; UPA00331; UER00451.
DR Proteomes; UP000001917; Chromosome.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.160.750; -; 1.
DR Gene3D; 3.30.360.110; S-adenosylmethionine decarboxylase domain; 1.
DR HAMAP; MF_00464; AdoMetDC_1; 1.
DR InterPro; IPR042286; AdoMetDC_C.
DR InterPro; IPR003826; AdoMetDC_fam_prok.
DR InterPro; IPR042284; AdoMetDC_N.
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:UP000001917};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW 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..62
FT /note="S-adenosylmethionine decarboxylase beta chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT /id="PRO_5023492311"
FT CHAIN 63..127
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT /id="PRO_5023492310"
FT ACT_SITE 63
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT ACT_SITE 68
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT ACT_SITE 83
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT SITE 62..63
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT MOD_RES 63
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
SQ SEQUENCE 127 AA; 14057 MW; 2CDA9E59300D1A55 CRC64;
MDTMGRHVIA ELWECDPERL NDVHGIERAM VTAALEAGAE VREVAFHKFA PQGVSGVVII
SESHLTIHSF PEHGYASIDV YTCGDRIDPN VACDYITKYL GAKRLEAIEL PRGVGQIQVH
DVKVRAF
//
