SPEA_SALTI
ID SPEA_SALTI Reviewed; 658 AA.
AC P60658; Q8XFQ5;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Biosynthetic arginine decarboxylase {ECO:0000255|HAMAP-Rule:MF_01417};
DE Short=ADC {ECO:0000255|HAMAP-Rule:MF_01417};
DE EC=4.1.1.19 {ECO:0000255|HAMAP-Rule:MF_01417};
GN Name=speA {ECO:0000255|HAMAP-Rule:MF_01417};
GN OrderedLocusNames=STY3240, t2999;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
CC -!- FUNCTION: Catalyzes the biosynthesis of agmatine from arginine.
CC {ECO:0000255|HAMAP-Rule:MF_01417}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-arginine = agmatine + CO2; Xref=Rhea:RHEA:17641,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:58145; EC=4.1.1.19; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01417};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01417};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01417};
CC -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC agmatine from L-arginine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01417}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC SpeA subfamily. {ECO:0000255|HAMAP-Rule:MF_01417}.
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DR EMBL; AL513382; CAD02911.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO70551.1; -; Genomic_DNA.
DR RefSeq; NP_457479.1; NC_003198.1.
DR RefSeq; WP_001278580.1; NZ_WSUR01000049.1.
DR AlphaFoldDB; P60658; -.
DR SMR; P60658; -.
DR STRING; 220341.16504164; -.
DR EnsemblBacteria; AAO70551; AAO70551; t2999.
DR KEGG; stt:t2999; -.
DR KEGG; sty:STY3240; -.
DR PATRIC; fig|220341.7.peg.3303; -.
DR eggNOG; COG1166; Bacteria.
DR HOGENOM; CLU_027243_1_0_6; -.
DR OMA; AVEYTQH; -.
DR UniPathway; UPA00186; UER00284.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR GO; GO:0009446; P:putrescine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06830; PLPDE_III_ADC; 1.
DR Gene3D; 2.40.37.10; -; 1.
DR Gene3D; 3.20.20.10; -; 1.
DR HAMAP; MF_01417; SpeA; 1.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR040634; Arg_decarb_HB.
DR InterPro; IPR041128; Arg_decarbox_C.
DR InterPro; IPR002985; Arg_decrbxlase.
DR InterPro; IPR022657; De-COase2_CS.
DR InterPro; IPR022644; De-COase2_N.
DR InterPro; IPR022653; De-COase2_pyr-phos_BS.
DR InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR InterPro; IPR029066; PLP-binding_barrel.
DR PANTHER; PTHR43295; PTHR43295; 1.
DR Pfam; PF17810; Arg_decarb_HB; 1.
DR Pfam; PF17944; Arg_decarbox_C; 1.
DR Pfam; PF02784; Orn_Arg_deC_N; 1.
DR PIRSF; PIRSF001336; Arg_decrbxlase; 1.
DR PRINTS; PR01180; ARGDCRBXLASE.
DR PRINTS; PR01179; ODADCRBXLASE.
DR SUPFAM; SSF50621; SSF50621; 1.
DR SUPFAM; SSF51419; SSF51419; 1.
DR TIGRFAMs; TIGR01273; speA; 1.
DR PROSITE; PS00878; ODR_DC_2_1; 1.
DR PROSITE; PS00879; ODR_DC_2_2; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Magnesium; Metal-binding; Polyamine biosynthesis;
KW Putrescine biosynthesis; Pyridoxal phosphate; Spermidine biosynthesis.
FT CHAIN 1..658
FT /note="Biosynthetic arginine decarboxylase"
FT /id="PRO_0000149975"
FT BINDING 307..317
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
FT MOD_RES 127
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
SQ SEQUENCE 658 AA; 73833 MW; 8A689D85DB85D6CF CRC64;
MSDDMSMGSP SSAGEQGVLR SMQEVAMSSQ EASKMLRTYN IAWWGNNYYD VNELGHISVC
PDPDVPEARV DLAKLVKARE AQGQRLPALF CFPQILQHRL RSINAAFKRA RESYGYNGDY
FLVYPIKVNQ HRRVIESLIH SGEPLGLEAG SKAELMAVLA HAGMTRSVIV CNGYKDREYI
RLALIGEKMG HKVYLVIEKM SEIAIVLEEA ERLNVVPRLG VRARLASQGS GKWQSSGGEK
SKFGLAATQV LQLVETLRDA GRLDSLQLLH FHLGSQMANI RDIATGVRES ARFYVELHKL
GVNIQCFDVG GGLGVDYEGT RSQSDCSVNY GLNEYANNII WAIGDACEEH GLPHPTVITE
SGRAVTAHHT VLVSNIIGVE RNEYTDPTAP AEDAPRALQN LWETWQEMHK PGTRRSLREW
LHDSQMDLHD IHIGYSSGAF SLQERAWAEQ LYLSMCHEVQ KQLDPQNRAH RPIIDELQER
MADKMYVNFS LFQSMPDAWG IDQLFPVLPL EGLDQVPERR AVLLDITCDS DGAIDHYIDG
DGIATTMPMP EYDPENPPML GFFMVGAYQE ILGNMHNLFG DTEAVDVFVF PDGSVEVELS
DEGDTVADML QYVQLDPKTL LTHFRDQVKQ TDLDDALQQQ FLEEFEAGLY GYTYLEDE
