ID   SPEA_PROM0              Reviewed;         648 AA.
AC   A3PA96;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=P9301_00481;
OS   Prochlorococcus marinus (strain MIT 9301).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9301;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000576; ABO16671.1; -; Genomic_DNA.
DR   RefSeq; WP_011862076.1; NC_009091.1.
DR   AlphaFoldDB; A3PA96; -.
DR   SMR; A3PA96; -.
DR   STRING; 167546.P9301_00481; -.
DR   EnsemblBacteria; ABO16671; ABO16671; P9301_00481.
DR   KEGG; pmg:P9301_00481; -.
DR   eggNOG; COG1166; Bacteria.
DR   HOGENOM; CLU_027243_1_0_3; -.
DR   OMA; AVEYTQH; -.
DR   UniPathway; UPA00186; UER00284.
DR   Proteomes; UP000001430; 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; 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; Reference proteome; Spermidine biosynthesis.
FT   CHAIN           1..648
FT                   /note="Biosynthetic arginine decarboxylase"
FT                   /id="PRO_1000024258"
FT   BINDING         291..301
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
FT   MOD_RES         109
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
SQ   SEQUENCE   648 AA;  73366 MW;  7B3791D58CCC947E CRC64;
     MTNFEPKKLK NVWTIEDSIS TYNIDKWGDK YFSINSKGNI SVTKDIKSEN KIDLFKLVKE
     LKSREINPPL IIRFNDILKD RINALHDSFF KAIKTYKYKN IYQGVFPVKC NQQKNVLEKI
     IDFGSQWNFG LEVGSKSELL IGLALLENHN SLLICNGYKD KKYIEIATLA RKLGKNPIIV
     IEQRDEVKRI IQAVQELNAT PLIGIRAKLS SKSSGRWGKS IGDNSKFGLS IPEIMLTIKE
     LKEANLINEM KLLHFHIGSQ ISDIAVIKDA LQEASQIYVE LCKLGAPMQY IDVGGGLGID
     FDGTKTSSNT STNYSLQNYA NDVIATIKDS CELNNIKHPT IISESGRAII SHCSVLIFNV
     LGTSHVSSKL QIFDKKNQQL IISNLLETYY ELKKLKNKKI NLSQIIELWN DAKKFKEDCL
     VAFRLGFLSL AERAYAEELA WACAKEISNN LNNDEINHPD LSEITETLAS TYYANLSIFK
     SIPDSWAINQ IFPIVPIHRH LEEPFCKGNF ADLTCDSDGK LNNFIDDGKI KSLLNLHEPE
     KDKDYLIGIF MTGAYQEALG NLHNLFGSTN VVHIDINQDD SYKVKNIIKE DSKSEILQLL
     DYSSASLVES IRINTESAID QKKLTIEEAR KLMDQIEISL RKSSYLSE