ID   SPEA_GEOSM              Reviewed;         635 AA.
AC   C6E3V4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
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}; OrderedLocusNames=GM21_1309;
OS   Geobacter sp. (strain M21).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter; unclassified Geobacter.
OX   NCBI_TaxID=443144;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M21;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Lovley D.;
RT   "Complete sequence of Geobacter sp. M21.";
RL   Submitted (JUL-2009) 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;
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; CP001661; ACT17369.1; -; Genomic_DNA.
DR   RefSeq; WP_015836621.1; NC_012918.1.
DR   AlphaFoldDB; C6E3V4; -.
DR   SMR; C6E3V4; -.
DR   STRING; 443144.GM21_1309; -.
DR   EnsemblBacteria; ACT17369; ACT17369; GM21_1309.
DR   KEGG; gem:GM21_1309; -.
DR   eggNOG; COG1166; Bacteria.
DR   HOGENOM; CLU_027243_1_0_7; -.
DR   OMA; AVEYTQH; -.
DR   UniPathway; UPA00186; UER00284.
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; 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   Pyridoxal phosphate; Spermidine biosynthesis.
FT   CHAIN           1..635
FT                   /note="Biosynthetic arginine decarboxylase"
FT                   /id="PRO_1000215247"
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;  71705 MW;  588FE255ED8B7EB4 CRC64;
     MAKWTINDSS KIYNIDNWGA ELFSINKKGN VCVHPSPNSK YSIDLKVLVD DLIKRKIKPP
     ILLRFMNILE GRIASISRVF KNAISDNNYP AKYQTFYPIK VNQQRQVVEA IANFGKKYNI
     GLEVGSKPEL VAAISMSTGN NLPILCNGYK DTEFIETVLF ATRVGYDITI VVEKLFELEK
     IVEVSKRTGI VPKLGIRVKL SSKGIGKWST SGGDDAKFGL RISELIAAIE MLKQNDMLDS
     VKLLHFHVGS QITKIDKIKN ALIEGTRIYA EMRKLGVNLE FLDIGGGLGV DYDGSKSSYF
     SSVNYSLEEY ANDVIYQVKN ICDDAGVPCP NIISESGRAT VAHYSVLVTD VLNNNTQTLM
     PDFESILTES EKLSPTVKKL VDIYKSIDKH SLREDYHDTI QLIQESVSLF NLGYLNMAER
     ANAEWICSKI IRKINSIVEK MKPIPDELQN FQLSLRQTYF ANFSLFQSIP DSWAIDQLFP
     IVPIQRLDEK PDVLTSIADI TCDSDGEITS FVGENGRTKA LPLHKIKVDE QYYIGFFLIG
     AYQEILGDMH NLFGDTNAVH ITFNKKTNYK IDTVITGDAT WESLKYVQYD SQEILKRVRN
     NLEKDVSLQK VSIEESSHFL ELLDKTLQSY TYLGE