SPEH_BACSU
ID SPEH_BACSU Reviewed; 126 AA.
AC O34426;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 140.
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}; Synonyms=speD, ytcF;
GN OrderedLocusNames=BSU29010;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO N-TERMINUS.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP FUNCTION, MUTAGENESIS OF SER-63, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=10844697; DOI=10.1046/j.1365-2958.2000.01930.x;
RA Sekowska A., Coppee J.-Y., Le Caer J.-P., Martin-Verstraete I., Danchin A.;
RT "S-adenosylmethionine decarboxylase of Bacillus subtilis is closely related
RT to archaebacterial counterparts.";
RL Mol. Microbiol. 36:1135-1147(2000).
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 ECO:0000269|PubMed:10844697}.
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 Note=Binds 1 pyruvoyl group covalently per subunit.;
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 -!- DISRUPTION PHENOTYPE: Proteome analysis shows that a mutant
CC overexpresses SAM synthase by comparison to wild-type.
CC {ECO:0000269|PubMed:10844697}.
CC -!- SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00464}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC00356.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF008220; AAC00356.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB14861.2; -; Genomic_DNA.
DR PIR; C69989; C69989.
DR RefSeq; NP_390779.2; NC_000964.3.
DR RefSeq; WP_003223584.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O34426; -.
DR SMR; O34426; -.
DR STRING; 224308.BSU29010; -.
DR PaxDb; O34426; -.
DR EnsemblBacteria; CAB14861; CAB14861; BSU_29010.
DR GeneID; 50136637; -.
DR GeneID; 64304631; -.
DR GeneID; 936773; -.
DR KEGG; bsu:BSU29010; -.
DR PATRIC; fig|224308.179.peg.3150; -.
DR eggNOG; COG1586; Bacteria.
DR InParanoid; O34426; -.
DR OMA; HTWPEKG; -.
DR PhylomeDB; O34426; -.
DR BioCyc; BSUB:BSU29010-MON; -.
DR BioCyc; MetaCyc:MON-11536; -.
DR UniPathway; UPA00331; UER00451.
DR PRO; PR:O34426; -.
DR Proteomes; UP000001570; 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 Autocatalytic cleavage; Decarboxylase; Lyase; Polyamine biosynthesis;
KW Pyruvate; Reference proteome; S-adenosyl-L-methionine; Schiff base;
KW Spermidine biosynthesis; Zymogen.
FT CHAIN 1..62
FT /note="S-adenosylmethionine decarboxylase beta chain"
FT /evidence="ECO:0000305"
FT /id="PRO_0000030101"
FT CHAIN 63..126
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /evidence="ECO:0000305"
FT /id="PRO_0000030102"
FT ACT_SITE 63
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00464"
FT ACT_SITE 68
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00464"
FT ACT_SITE 83
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00464"
FT SITE 62..63
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00464"
FT MOD_RES 63
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00464"
FT MUTAGEN 63
FT /note="S->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:10844697"
SQ SEQUENCE 126 AA; 13873 MW; 98EDA88C6DB4D4FC CRC64;
METMGRHVIS ELWGCDFDKL NDMDFIEKTF VNAALKSGAE VREVAFHKFA PQGVSGVVII
SESHLTIHSF PEHGYASIDV YTCGDLDPNV AADYIAEALH ADTRENIEIP RGMGPVQIKQ
AQAKVL
