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Database: UniProt
Entry: L0A932_CALLD
LinkDB: L0A932_CALLD
Original site: L0A932_CALLD 
ID   L0A932_CALLD            Unreviewed;       149 AA.
AC   L0A932;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 51.
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=Calag_0621 {ECO:0000313|EMBL:AFZ70376.1};
OS   Caldisphaera lagunensis (strain DSM 15908 / JCM 11604 / ANMR 0165 /
OS   IC-154).
OC   Archaea; Thermoproteota; Thermoprotei; Acidilobales; Caldisphaeraceae;
OC   Caldisphaera.
OX   NCBI_TaxID=1056495 {ECO:0000313|EMBL:AFZ70376.1, ECO:0000313|Proteomes:UP000010469};
RN   [1] {ECO:0000313|EMBL:AFZ70376.1, ECO:0000313|Proteomes:UP000010469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15908 / JCM 11604 / IC-154
RC   {ECO:0000313|Proteomes:UP000010469};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Teshima H.,
RA   Kyrpides N., Mavromatis K., Ivanova N., 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., Spring S., Schroeder M., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "Complete genome of Caldisphaera lagunensis DSM 15908.";
RL   Submitted (MAR-2012) 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}.
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DR   EMBL; CP003378; AFZ70376.1; -; Genomic_DNA.
DR   RefSeq; WP_015232274.1; NC_019791.1.
DR   AlphaFoldDB; L0A932; -.
DR   STRING; 1056495.Calag_0621; -.
DR   GeneID; 14211881; -.
DR   KEGG; clg:Calag_0621; -.
DR   eggNOG; arCOG00279; Archaea.
DR   HOGENOM; CLU_125470_2_1_2; -.
DR   InParanoid; L0A932; -.
DR   OMA; VYTCGEH; -.
DR   OrthoDB; 114016at2157; -.
DR   UniPathway; UPA00331; UER00451.
DR   Proteomes; UP000010469; 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; 3.60.90.10; 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:UP000010469};
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}; Spermidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00464};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_00464}.
FT   CHAIN           1..77
FT                   /note="S-adenosylmethionine decarboxylase beta chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT                   /id="PRO_5023295549"
FT   CHAIN           78..149
FT                   /note="S-adenosylmethionine decarboxylase alpha chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT                   /id="PRO_5023295548"
FT   ACT_SITE        78
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT   ACT_SITE        83
FT                   /note="Proton acceptor; for processing activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT   ACT_SITE        98
FT                   /note="Proton donor; for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT   SITE            77..78
FT                   /note="Cleavage (non-hydrolytic); by autolysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT   MOD_RES         78
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
SQ   SEQUENCE   149 AA;  17048 MW;  84412CE1701676D3 CRC64;
     MNLEVNEESR SDVDFIVGKH VYGSLYGLKP EIADDEELIR QTVLDAVKAA NATLIQLMSW
     KIPGIKGGVS VMALVNESHI VIHTWKEYRY ATVDVYTCGN HTNPEKAYKL IVERLKPQYY
     SYNYADRTQF PTSSPVKRDE MRIETATPY
//
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