ID   SPEA_RHOBA              Reviewed;         668 AA.
AC   Q7UTS2;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, 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}; OrderedLocusNames=RB3708;
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA   Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA   Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT   1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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   -!- 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; BX294139; CAD73363.1; -; Genomic_DNA.
DR   RefSeq; NP_865678.1; NC_005027.1.
DR   RefSeq; WP_011119511.1; NC_005027.1.
DR   AlphaFoldDB; Q7UTS2; -.
DR   SMR; Q7UTS2; -.
DR   STRING; 243090.RB3708; -.
DR   EnsemblBacteria; CAD73363; CAD73363; RB3708.
DR   KEGG; rba:RB3708; -.
DR   PATRIC; fig|243090.15.peg.1723; -.
DR   eggNOG; COG1166; Bacteria.
DR   HOGENOM; CLU_027243_1_0_0; -.
DR   InParanoid; Q7UTS2; -.
DR   OrthoDB; 9802658at2; -.
DR   Proteomes; UP000001025; 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; 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   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..668
FT                   /note="Biosynthetic arginine decarboxylase"
FT                   /id="PRO_0000149974"
FT   BINDING         286..296
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
FT   MOD_RES         105
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
SQ   SEQUENCE   668 AA;  74081 MW;  3851560B071E60A9 CRC64;
     MSSVLDSKWT RSDASKTYDI DRWGAGYFSI SDAGTVLVSP DRDPSQSIDL KELVDRLGQR
     NLDLPILLRF NGILRDRLRE LDRCFKNAIH DHKYQSRYRC VFPIKVNQQR EVVQQIVSEG
     ARLGFGIEAG SKPELVAAVA MGDANVPIVC NGFKDEEFIR LALLAQRLGR NVLPVVEKVS
     ELDLILDVAK DIGVRPTIGM RVKLATRGSG RWQASGGYRS KFGLTVAELL AQLDRLIAMD
     MGDCLQLLHF HVGSQIGNIR QLKSAILEAA RIYVDLVRRG AGMRYLDVGG GLGVDYDGSR
     SDSESSMNYT MQEYANDVVY HTQTVCDEAG VPHPELISES GRAVAAHHSV LVMETLGVTS
     QGVANLPCWA KVEGEPVSPD HGGIEMDSVG AIETSEMEGP PESYEQPVHD LWVGYVNMTQ
     ANMMETFHDA QVALDLCMNL FSGGYLPLEQ RVAAENLYFA ICHRVRELAE SMKERPDDLK
     HLDRMLSDIY FANFSLFQSM PDSWAIDQLF PIMPIHRLLE KPSRHAVLGD ITCDSDGKVD
     AFVCGGGRQR TLMLHPLKSG EPYQLAVFMV GAYQEILGDL HNLFGDTHAV HVDIEDGVTK
     VRSIVKGDTV SEVLGYVQYE DRELIENLQE SVESAIGNGH IDHQQAGETV AAYERALSGY
     TYLSTRTK
//