SPEH_AQUAE
ID SPEH_AQUAE Reviewed; 135 AA.
AC O66615;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=S-adenosylmethionine decarboxylase proenzyme {ECO:0000255|HAMAP-Rule:MF_00464};
DE Short=AdoMetDC {ECO:0000255|HAMAP-Rule:MF_00464};
DE Short=SAMDC {ECO:0000255|HAMAP-Rule:MF_00464};
DE EC=4.1.1.50 {ECO:0000255|HAMAP-Rule:MF_00464};
DE Contains:
DE RecName: Full=S-adenosylmethionine decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_00464};
DE Contains:
DE RecName: Full=S-adenosylmethionine decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_00464};
DE Flags: Precursor;
GN Name=speH {ECO:0000255|HAMAP-Rule:MF_00464}; OrderedLocusNames=aq_254;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RC STRAIN=VF5;
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of the adenosylmethionine decarboxylase (aq_254) from
RT Aquifex aeolicus VF5.";
RL Submitted (OCT-2007) to the PDB data bank.
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_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:0000255|HAMAP-Rule:MF_00464};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00464};
CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00464}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged as a
CC dimer of alpha/beta heterodimers. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00464}.
CC -!- SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00464}.
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DR EMBL; AE000657; AAC06577.1; -; Genomic_DNA.
DR PIR; C70323; C70323.
DR RefSeq; NP_213175.1; NC_000918.1.
DR RefSeq; WP_010880113.1; NC_000918.1.
DR PDB; 2III; X-ray; 2.30 A; A=1-135.
DR PDBsum; 2III; -.
DR AlphaFoldDB; O66615; -.
DR SMR; O66615; -.
DR STRING; 224324.aq_254; -.
DR EnsemblBacteria; AAC06577; AAC06577; aq_254.
DR KEGG; aae:aq_254; -.
DR PATRIC; fig|224324.8.peg.209; -.
DR eggNOG; COG1586; Bacteria.
DR HOGENOM; CLU_125470_2_3_0; -.
DR InParanoid; O66615; -.
DR OMA; HTWPEKG; -.
DR OrthoDB; 1613081at2; -.
DR BRENDA; 4.1.1.50; 396.
DR UniPathway; UPA00331; UER00451.
DR EvolutionaryTrace; O66615; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IBA:GO_Central.
DR GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008295; P:spermidine biosynthetic process; IBA:GO_Central.
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 PANTHER; PTHR33866; PTHR33866; 1.
DR Pfam; PF02675; AdoMet_dc; 1.
DR SUPFAM; SSF56276; SSF56276; 1.
DR TIGRFAMs; TIGR03330; SAM_DCase_Bsu; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Decarboxylase; Lyase;
KW Polyamine biosynthesis; Pyruvate; Reference proteome;
KW S-adenosyl-L-methionine; Schiff base; Spermidine biosynthesis; Zymogen.
FT CHAIN 1..63
FT /note="S-adenosylmethionine decarboxylase beta chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00464"
FT /id="PRO_0000030079"
FT CHAIN 64..135
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00464"
FT /id="PRO_0000030080"
FT ACT_SITE 64
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00464"
FT ACT_SITE 69
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00464"
FT ACT_SITE 84
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00464"
FT SITE 63..64
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00464"
FT MOD_RES 64
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00464"
FT STRAND 3..15
FT /evidence="ECO:0007829|PDB:2III"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:2III"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:2III"
FT HELIX 24..37
FT /evidence="ECO:0007829|PDB:2III"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:2III"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2III"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:2III"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:2III"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:2III"
FT STRAND 76..85
FT /evidence="ECO:0007829|PDB:2III"
FT HELIX 87..101
FT /evidence="ECO:0007829|PDB:2III"
FT STRAND 104..116
FT /evidence="ECO:0007829|PDB:2III"
SQ SEQUENCE 135 AA; 15200 MW; 3C048331A9118872 CRC64;
MAKTLGLHIL ADLYGVDADK IDRVEDIREL LEGAVKYANL TKISSHYYQF QPHGATGVVL
LAESHISIHT WPEHGLATVD VYTCGDPSKA YRAMDYIITQ LNPKRIDKQV HERGIVEEES
NQSEAEKLRS ILLQV
