SPEH_THEMA
ID SPEH_THEMA Reviewed; 130 AA.
AC Q9WZC3;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=S-adenosylmethionine decarboxylase proenzyme;
DE Short=AdoMetDC;
DE Short=SAMDC;
DE EC=4.1.1.50;
DE Contains:
DE RecName: Full=S-adenosylmethionine decarboxylase beta chain;
DE Contains:
DE RecName: Full=S-adenosylmethionine decarboxylase alpha chain;
DE Flags: Precursor;
GN Name=speH; OrderedLocusNames=TM_0655;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-63,
RP SUBUNIT, SELF-PROCESSING, ACTIVE SITES, AND MUTAGENESIS OF SER-55; SER-63;
RP HIS-68 AND CYS-83.
RX PubMed=15150268; DOI=10.1074/jbc.m403369200;
RA Toms A.V., Kinsland C., McCloskey D.E., Pegg A.E., Ealick S.E.;
RT "Evolutionary links as revealed by the structure of Thermotoga maritima S-
RT adenosylmethionine decarboxylase.";
RL J. Biol. Chem. 279:33837-33846(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS).
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of S-adenosylmethionine decarboxylase proenzyme (tm0655)
RT from Thermotoga maritima at 1.2-A resolution.";
RL Submitted (MAR-2005) 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:0000250}.
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 -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000305};
CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000305};
CC -!- PATHWAY: Amine and polyamine biosynthesis; S-adenosylmethioninamine
CC biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine:
CC step 1/1.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged as a
CC dimer of alpha/beta heterodimers. {ECO:0000269|PubMed:15150268}.
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 (Probable). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 1
CC subfamily. {ECO:0000305}.
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DR EMBL; AE000512; AAD35739.1; -; Genomic_DNA.
DR PIR; D72348; D72348.
DR RefSeq; NP_228464.1; NC_000853.1.
DR RefSeq; WP_004081137.1; NZ_CP011107.1.
DR PDB; 1TLU; X-ray; 1.55 A; A/B=1-130.
DR PDB; 1TMI; X-ray; 1.70 A; A/B=1-130.
DR PDB; 1VR7; X-ray; 1.20 A; A/B=1-130.
DR PDB; 3IWB; X-ray; 2.06 A; A/C=64-130, B/D=1-62.
DR PDB; 3IWC; X-ray; 1.90 A; A/C=64-130, B/D=1-62.
DR PDB; 3IWD; X-ray; 1.90 A; A/C=64-130, B/D=1-62.
DR PDBsum; 1TLU; -.
DR PDBsum; 1TMI; -.
DR PDBsum; 1VR7; -.
DR PDBsum; 3IWB; -.
DR PDBsum; 3IWC; -.
DR PDBsum; 3IWD; -.
DR AlphaFoldDB; Q9WZC3; -.
DR SMR; Q9WZC3; -.
DR STRING; 243274.THEMA_01390; -.
DR EnsemblBacteria; AAD35739; AAD35739; TM_0655.
DR KEGG; tma:TM0655; -.
DR eggNOG; COG1586; Bacteria.
DR InParanoid; Q9WZC3; -.
DR OMA; HTWPEKG; -.
DR OrthoDB; 1613081at2; -.
DR BRENDA; 4.1.1.50; 6331.
DR UniPathway; UPA00331; UER00451.
DR EvolutionaryTrace; Q9WZC3; -.
DR Proteomes; UP000008183; 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 Gene3D; 3.30.160.750; -; 1.
DR Gene3D; 3.30.360.110; -; 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 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..62
FT /note="S-adenosylmethionine decarboxylase beta chain"
FT /evidence="ECO:0000305"
FT /id="PRO_0000030123"
FT CHAIN 63..130
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /evidence="ECO:0000305"
FT /id="PRO_0000030124"
FT ACT_SITE 63
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000250"
FT ACT_SITE 68
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000305|PubMed:15150268"
FT ACT_SITE 83
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000305|PubMed:15150268"
FT SITE 62..63
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000305"
FT MOD_RES 63
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000305"
FT MUTAGEN 55
FT /note="S->A: Cleaves more rapidly than the wild-type."
FT /evidence="ECO:0000269|PubMed:15150268"
FT MUTAGEN 63
FT /note="S->A: Loss of processing."
FT /evidence="ECO:0000269|PubMed:15150268"
FT MUTAGEN 68
FT /note="H->A: Cleaves much more slowly than the wild-type,
FT but the addition of hydroxylamine which is known to cleave
FT ester bonds leads to the cleavage of this mutant."
FT /evidence="ECO:0000269|PubMed:15150268"
FT MUTAGEN 83
FT /note="C->A: Cleaves more rapidly than the wild-type."
FT /evidence="ECO:0000269|PubMed:15150268"
FT STRAND 3..14
FT /evidence="ECO:0007829|PDB:1VR7"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:1VR7"
FT HELIX 23..37
FT /evidence="ECO:0007829|PDB:1VR7"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:1VR7"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1VR7"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:1VR7"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:1VR7"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:1VR7"
FT STRAND 75..84
FT /evidence="ECO:0007829|PDB:1VR7"
FT HELIX 89..100
FT /evidence="ECO:0007829|PDB:1VR7"
FT STRAND 103..114
FT /evidence="ECO:0007829|PDB:1VR7"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:1VR7"
SQ SEQUENCE 130 AA; 14785 MW; 7659FE20A2019928 CRC64;
MKSLGRHLVA EFYECDREVL DNVQLIEQEM KQAAYESGAT IVTSTFHRFL PYGVSGVVVI
SESHLTIHTW PEYGYAAIDL FTCGEDVDPW KAFEHLKKAL KAKRVHVVEH ERGRYDEIGI
PEDSPHKAAV
