ID   SPEA_ECOL6              Reviewed;         658 AA.
AC   Q8FE34;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Biosynthetic arginine decarboxylase;
DE            Short=ADC;
DE            EC=4.1.1.19;
GN   Name=speA; OrderedLocusNames=c3524;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Catalyzes the biosynthesis of agmatine from arginine.
CC       {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC       agmatine from L-arginine: step 1/1.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       SpeA subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN81972.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN81972.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001295380.1; NC_004431.1.
DR   AlphaFoldDB; Q8FE34; -.
DR   SMR; Q8FE34; -.
DR   STRING; 199310.c3524; -.
DR   EnsemblBacteria; AAN81972; AAN81972; c3524.
DR   GeneID; 66673180; -.
DR   KEGG; ecc:c3524; -.
DR   eggNOG; COG1166; Bacteria.
DR   HOGENOM; CLU_027243_1_0_6; -.
DR   OMA; AVEYTQH; -.
DR   UniPathway; UPA00186; UER00284.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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; Periplasm;
KW   Polyamine biosynthesis; Putrescine biosynthesis; Pyridoxal phosphate;
KW   Spermidine biosynthesis.
FT   CHAIN           1..658
FT                   /note="Biosynthetic arginine decarboxylase"
FT                   /id="PRO_0000149961"
FT   BINDING         307..317
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         127
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   658 AA;  73886 MW;  87106BF8727B6EE2 CRC64;
     MSDDMSMGLP SSAGEHGVLR SMQEVAMSSQ EASKMLRTYN IAWWGNNYYD VNELGHISVC
     PDPDVPEARV DLAQLVKTRE AQGQRLPALF CFPQILQHRL RSINAAFKRA RESYGYNGDY
     FLVYPIKVNQ HRRVIESLIH SGEPLGLEAG SKAELMAVLA HAGMTRSVIV CNGYKDREYI
     RLALIGEKMG HKVYLVIEKM SEIAIVLDEA ERLNVVPRLG VRARLASQGS GKWQSSGGEK
     SKFGLAATQV LQLVETLREA GRLDSLQLLH FHLGSQMANI RDIATGVRES ARFYVELHKL
     GVNIQCFDVG GGLGVDYEGT RSQSDCSVNY GLNEYANNII WAIGDACEEN GLPHPTVITE
     SGRAVTAHHT VLVSNIIGVE RNEYTVPTAP AEDAPRALQS MWETWQEMHE PGTRRSLREW
     LHDSQMDLHD IHIGYSSGTF SLQERAWAEQ LYLSMCHEVQ KQLDPQNRAH RPIIDELQER
     MADKMYVNFS LFQSMPDAWG IDQLFPVLPL EGLDQVPERR AVLLDITCDS DGAIDHYIDG
     DGIATTMPMP EYDPENPPML GFFMVGAYQE ILGNMHNLFG DTEAVDVFVF PDGSVEVELS
     DEGDTVADML QYVQLDPKTL LTQFRDQVKK TDLDAELQQQ FLEEFEAGLY GYTYLEDE