ID   SPEA_GEOMG              Reviewed;         635 AA.
AC   Q39X78;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 104.
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=Gmet_0904;
OS   Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=269799;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53774 / DSM 7210 / GS-15;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Geobacter metallireducens GS-15.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000255|HAMAP-
CC         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; CP000148; ABB31146.1; -; Genomic_DNA.
DR   RefSeq; WP_004513934.1; NC_007517.1.
DR   AlphaFoldDB; Q39X78; -.
DR   SMR; Q39X78; -.
DR   STRING; 269799.Gmet_0904; -.
DR   KEGG; gme:Gmet_0904; -.
DR   eggNOG; COG1166; Bacteria.
DR   HOGENOM; CLU_027243_1_0_7; -.
DR   UniPathway; UPA00186; UER00284.
DR   Proteomes; UP000007073; 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:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06830; PLPDE_III_ADC; 1.
DR   Gene3D; 1.10.287.3440; -; 1.
DR   Gene3D; 1.20.58.930; -; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 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   NCBIfam; TIGR01273; speA; 1.
DR   PANTHER; PTHR43295; ARGININE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43295:SF9; BIOSYNTHETIC ARGININE DECARBOXYLASE; 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; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 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   Pyridoxal phosphate; Reference proteome; Spermidine biosynthesis.
FT   CHAIN           1..635
FT                   /note="Biosynthetic arginine decarboxylase"
FT                   /id="PRO_1000068490"
FT   BINDING         282..292
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
FT   MOD_RES         100
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
SQ   SEQUENCE   635 AA;  71521 MW;  689186DAE924266B CRC64;
     MERWSINDSA KIYNLPNWGA DLFSINKKGN VCVHPSPTSK HSIDLRALVD DLIKRKIKPP
     ILLRFMDVLQ GRIAAINRAF KYAIDENDYP STYQTFYPIK VNQQRQVVEA IAKFGKRYNI
     GIEVGSKPEL VIGISFATGN GIPIICNGYK DKEYIETVLY ATKIGYDITI VVEKMFELEK
     IIALSKKTGI KPKLGIRVKL SSKGTGKWAT SGGEDAKFGL RMSEIIAAIG LLEQNELLDS
     VKLIHFHIGS QITKIDKIKS ALIEGTRVYA EMRKLGVGIE YVDIGGGLGV DYDGSKSSYF
     SSVNYSIEEY ANDVIYQIKN ICEDAGVECP NIISESGRAT AAHYSVLVTN LLNTNTQNLM
     PDFEETLNGA EKLAPTVKKL VDIYKSIDRY SLREDYHDTV QLIQEAVSLF SLGYLTLAER
     AMAEWLHGKI LRKINGIVEK IKPIPEELQN FQLSLRQTYF ANFSLFQSIP DSWAIDQLFP
     IVPIQRLNQK PDVMASIADI TCDSDGEITS FVGENGRTKY LPLHKIRKDE DYFVGFFLIG
     AYQEILGDMH NLFGDTNAVH VTFNKKTGYK IDTVINGDAT WESLKYVQYK GPEILKHVRD
     TMEKDVALRK VSIEESSHFL ELLDRTLLGY TYLGE
//