ID   SPE1_AVESA              Reviewed;         607 AA.
AC   P22220;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   13-SEP-2023, entry version 107.
DE   RecName: Full=Arginine decarboxylase;
DE            Short=ADC;
DE            Short=ARGDC;
DE            EC=4.1.1.19;
GN   Name=SPE1;
OS   Avena sativa (Oat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Poodae; Poeae; Poeae Chloroplast Group 1 (Aveneae type);
OC   Aveninae; Avena.
OX   NCBI_TaxID=4498;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 427-437.
RC   TISSUE=Leaf;
RX   PubMed=2266946; DOI=10.1007/bf00262438;
RA   Bell E., Malmberg R.L.;
RT   "Analysis of a cDNA encoding arginine decarboxylase from oat reveals
RT   similarity to the Escherichia coli arginine decarboxylase and evidence of
RT   protein processing.";
RL   Mol. Gen. Genet. 224:431-436(1990).
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; X56802; CAA40137.1; -; mRNA.
DR   PIR; S12265; S12265.
DR   AlphaFoldDB; P22220; -.
DR   SMR; P22220; -.
DR   BioCyc; MetaCyc:MONOMER-14981; -.
DR   BRENDA; 4.1.1.19; 588.
DR   SABIO-RK; P22220; -.
DR   UniPathway; UPA00186; UER00284.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC.
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   PANTHER; PTHR43295; ARGININE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43295:SF2; ARGININE DECARBOXYLASE 2; 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   1: Evidence at protein level;
KW   Decarboxylase; Direct protein sequencing; Lyase; Magnesium;
KW   Putrescine biosynthesis; Pyridoxal phosphate; Spermidine biosynthesis.
FT   CHAIN           1..607
FT                   /note="Arginine decarboxylase"
FT                   /id="PRO_0000149948"
FT   BINDING         290..300
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         104
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   607 AA;  66706 MW;  757114B2C02EF8A5 CRC64;
     MAKNYGDVYH VEGWGEPYFA VNKDGHLCVR IYGRETLPGQ EIDVLSVIEQ ATSADGTGKK
     LQFPMILRFP DVLRHRINSL HTAFANAIKY TQYGSVYQGV FPVKVNQHKD VVQDMVHFGY
     DHSYGLEAGS KPELLIAMSC LTKAKPGAYL VCNGYKDSAY VALALAARAM GLNVIIVLEM
     EEELDIVIEE SSKLGVEPVI GVRAKLLTKI PGHFGSTAGK HGKFGLPAEK IYEVAKKLKA
     LNKLHWLKLL HFHVGSMIPT TDIVFKAASE ASDIYCALVK EYGVETMTTL DCGGGLGVDY
     DGTRSGSSDM SVAYGLEEYA SSIVQAVRLK CDYHGVPHPV LCTESGRAMA SYHSMIILEA
     LSAIPEPKDD EDEATTEQLH GRIRDLSSKL QPTGLSMSSH AVHIKKHGIE MYKLGKKLSK
     SVTTDAHTIY NYHMNLSVFS LMPDYWGIQH LFPMMPVSRL DEKPTHKATL VDVTCDSDGK
     VDKFIRDTET MPLHPLDPKL GGYYVAVLLT GAYQEALSNK HNLFGGPSLV RVVGTGNGGA
     FNVEAALLGS TTEELIGTVS YDVKQDISSV IEERARENKV WEMVEKLVES GLHTMPYLAD
     YKPPPMA
//