SPE1_SOLLC
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 03-AUG-2022, entry version 110.
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.Solyc01g110440.2.1; -.
DR PaxDb; P49726; -.
DR eggNOG; ENOG502QTXD; Eukaryota.
DR BioCyc; MetaCyc:MON-14985; -.
DR UniPathway; UPA00186; UER00284.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; P49726; baseline.
DR GO; GO:0008792; F:arginine decarboxylase activity; IBA:GO_Central.
DR GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR GO; GO:0033388; P:putrescine biosynthetic process from arginine; IBA:GO_Central.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd06830; PLPDE_III_ADC; 1.
DR Gene3D; 2.40.37.10; -; 1.
DR Gene3D; 3.20.20.10; -; 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 PANTHER; PTHR43295; PTHR43295; 1.
DR Pfam; PF02784; Orn_Arg_deC_N; 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 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