ID   SPE1_SOLLC              Reviewed;         502 AA.
AC   P49726;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, entry version 117.
DE   RecName: Full=Arginine decarboxylase;
DE            Short=ADC;
DE            Short=ARGDC;
DE            EC=4.1.1.19;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pericarp;
RX   PubMed=8022938; DOI=10.1104/pp.103.3.829;
RA   Rastogi R., Dulson J., Rothstein S.J.;
RT   "Cloning of tomato (Lycopersicon esculentum Mill.) arginine decarboxylase
RT   gene and its expression during fruit ripening.";
RL   Plant Physiol. 103:829-834(1993).
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=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC       agmatine from L-arginine: step 1/1.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       SpeA subfamily. {ECO:0000305}.
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DR   EMBL; L16582; AAA61347.1; -; mRNA.
DR   PIR; JQ2341; JQ2341.
DR   AlphaFoldDB; P49726; -.
DR   SMR; P49726; -.
DR   STRING; 4081.P49726; -.
DR   PaxDb; 4081-Solyc01g110440-2-1; -.
DR   eggNOG; ENOG502QTXD; Eukaryota.
DR   InParanoid; P49726; -.
DR   BioCyc; MetaCyc:MONOMER-14985; -.
DR   UniPathway; UPA00186; UER00284.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; P49726; baseline and differential.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR   GO; GO:0009446; P:putrescine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd06830; PLPDE_III_ADC; 1.
DR   Gene3D; 1.20.58.930; -; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_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:SF7; ARGININE DECARBOXYLASE; 1.
DR   Pfam; PF02784; Orn_Arg_deC_N; 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   2: Evidence at transcript level;
KW   Decarboxylase; Lyase; Magnesium; Putrescine biosynthesis;
KW   Pyridoxal phosphate; Reference proteome; Spermidine biosynthesis.
FT   CHAIN           1..502
FT                   /note="Arginine decarboxylase"
FT                   /id="PRO_0000149951"
FT   BINDING         226..236
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         42
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   502 AA;  54581 MW;  628D32D4560E9A1F CRC64;
     MPLVVRFPDV LKNRLETLQS AFDMAINSQG YEAHYQGVYP VKCNQDRFVV EDIVKFGSPY
     RFGLEAGSKP ELLLAMNCLS KGSADALLVC NGFKDTEYIS LALVARKLLL NSVIVLEQEE
     ELDLVIDISR KMSVRPVIGL RAKLRTKHSG HFGSTSGEKG KFGLTTTQIL RVVKKLDESG
     MLDCLQLLHF HIGSQIPTTE LLADGVGEAT QIYSELVRLG AGMKFIDIGG GLGIDYDGSK
     SSNSDVSVCY SIEEYASAVV QAVLYVCDRK GGKHPVICSE SGRAIVSHHS ILIFEAVSAS
     TSHVSTQPSS GGLQSLVETL NEDARADYRN LSAAAVRGEY DTCLIYSDQL KQRCVEQFKD
     GSLDIEQLAA VDSICDWVSK AIGVADPVRT YHVNLSVFTS IPDFWGFSQL FPIVPIHRLD
     EKPTMRGILS DLTCDSDGKV DKFIGGESSL PLHEIGSGDG GRYYLGMFLG GAYEEALGGL
     HNLFGGPSVV RVMQSDSPHS FA
//