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Database: UniProt
Entry: A0A316GBY8_9RHOB
LinkDB: A0A316GBY8_9RHOB
Original site: A0A316GBY8_9RHOB 
ID   A0A316GBY8_9RHOB        Unreviewed;       139 AA.
AC   A0A316GBY8;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=S-adenosylmethionine decarboxylase {ECO:0000313|EMBL:PWK58441.1};
GN   ORFNames=C8D95_101255 {ECO:0000313|EMBL:PWK58441.1};
OS   Silicimonas algicola.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=1826607 {ECO:0000313|EMBL:PWK58441.1, ECO:0000313|Proteomes:UP000245390};
RN   [1] {ECO:0000313|EMBL:PWK58441.1, ECO:0000313|Proteomes:UP000245390}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 103371 {ECO:0000313|EMBL:PWK58441.1,
RC   ECO:0000313|Proteomes:UP000245390};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC         Evidence={ECO:0000256|ARBA:ARBA00001928};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PWK58441.1}.
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DR   EMBL; QGGV01000001; PWK58441.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316GBY8; -.
DR   KEGG; salo:EF888_02725; -.
DR   OrthoDB; 9793120at2; -.
DR   Proteomes; UP000245390; Unassembled WGS sequence.
DR   GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:InterPro.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.750; -; 1.
DR   Gene3D; 3.30.360.110; S-adenosylmethionine decarboxylase domain; 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   4: Predicted;
KW   Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245390};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270};
KW   Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   139 AA;  14998 MW;  3916C2BB72054F95 CRC64;
     MMDTGTLTPS HTQPGAPDHL VRRGPRAFAG VHLLIDVRNG RGFDDEARVR QAIVDCVSAC
     GATLLHLHTH RFSPHGITGV AVLAESHIAA HTWPEHGYAA FDIFMCGSGR PEEAIAVLAR
     AFETEDIGVR EVLRGEVTV
//
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