ID A0A1N6MWC8_9GAMM Unreviewed; 501 AA.
AC A0A1N6MWC8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Putative Adenosylmethionine decarboxylase {ECO:0000313|EMBL:SIP73146.1};
DE EC=4.1.1.50 {ECO:0000313|EMBL:SIP73146.1};
GN ORFNames=XIS1_1750038 {ECO:0000313|EMBL:SIP73146.1};
OS Xenorhabdus innexi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=290109 {ECO:0000313|EMBL:SIP73146.1, ECO:0000313|Proteomes:UP000196435};
RN [1] {ECO:0000313|Proteomes:UP000196435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGB1681 (deposited as PTA-6826 in the American Type Culture
RC Collection) {ECO:0000313|Proteomes:UP000196435};
RA Gaudriault S.;
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000256|ARBA:ARBA00001928};
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DR EMBL; FTLG01000085; SIP73146.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N6MWC8; -.
DR OrthoDB; 278697at2; -.
DR Proteomes; UP000196435; Unassembled WGS sequence.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0043412; P:macromolecule modification; IEA:UniProt.
DR GO; GO:0032259; P:methylation; IEA:InterPro.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.60.90.10; S-adenosylmethionine decarboxylase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003826; AdoMetDC_fam_prok.
DR InterPro; IPR002723; BpsA_C.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR016067; S-AdoMet_deCO2ase_core.
DR InterPro; IPR017716; S-AdoMet_deCOase_pro-enz.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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 Pfam; PF01861; BpsA_C; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF56276; S-adenosylmethionine decarboxylase; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:SIP73146.1};
KW Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317};
KW Reference proteome {ECO:0000313|Proteomes:UP000196435};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270};
KW Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 115..339
FT /note="N(4)-bis(aminopropyl)spermidine synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01861"
SQ SEQUENCE 501 AA; 57877 MW; D8293BB9AEAE0A48 CRC64;
MNILCTIKKN MNLEQPIEVL EKLFVYLYLN DCVSNKELSL KIGLPIPIVS AFKKELIKSN
LAENKGVFKL NSVGVKYVKD ELNYKQVNYN LYNKLSSSEE HEKFKVDLAN LLTPVYDSRP
RVNVLLDQAH ATLDTSIRRV MLLLRNPIVF KQKILFLGDD DLTSLALMMA FKKLGHYGHE
NIYVKDIDKE LLKFIENVAK ENNFTINTEY LNLKEPNKYV RSFDVILTDP PYTFSGLKLF
LSRAISFSKN DGSEILLSFG QKKPKENYEV QKLFSDQNLF IKNIHPQFNK YYGGSIIGNV
SDLYTLSTTK NTYPTISEHS DYSNKIYTGE INPRIKFYQC KSCKNRLTIG YGKDLLTIEQ
LIETGCSQCN GTKFQYQGQE KIHLPADTKQ FGTHIIIEMK NCESDKLKSI STIENMMMDI
SRQCNFNIIN CYFHQSESYG ISGAIIFAGS HFSIHTWPEY SYAAFDLLIY SDFNHQDTLI
RQLQNQLNSQ EYECKILQRG F
//
