ID   SPE2_THECC              Reviewed;         406 AA.
AC   O81160;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Arginine decarboxylase;
DE            Short=ADC;
DE            Short=ARGDC;
DE            EC=4.1.1.19;
DE   Flags: Fragment;
GN   Name=SPE2;
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ADC;
RX   PubMed=9787437; DOI=10.1093/oxfordjournals.molbev.a025859;
RA   Galloway G.L., Malmberg R.L., Price R.A.;
RT   "Phylogenetic utility of the nuclear gene arginine decarboxylase: an
RT   example from Brassicaceae.";
RL   Mol. Biol. Evol. 15:1312-1320(1998).
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; AF045666; AAC68511.1; -; Genomic_DNA.
DR   AlphaFoldDB; O81160; -.
DR   SMR; O81160; -.
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; 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; 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; SSF51419; SSF51419; 1.
DR   PROSITE; PS00878; ODR_DC_2_1; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Magnesium; Putrescine biosynthesis;
KW   Pyridoxal phosphate; Spermidine biosynthesis.
FT   CHAIN           <1..>406
FT                   /note="Arginine decarboxylase"
FT                   /id="PRO_0000149955"
FT   BINDING         192..202
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         8
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         406
SQ   SEQUENCE   406 AA;  44604 MW;  A736338EE8ADD4D6 CRC64;
     YQGVYPVKSN QDRFVVEDIV KFGSSFRFGL EAGSKPELLL AMSCLCKGNP EALLVCNGFK
     DAEYISLALL ARKLALKHVI VLEQEEEVDM VIDISQKLSV RPVIGVRAKL RTKHSGHFGS
     TSGEKGKFGL TTTQVLRVVK KLQDSGMLDC LQLLHFHIGS QIPSTALLSD GVGEAAQIYS
     ELVRLGARMK VVDFGGGLGI DYNGSKSGDS DLSVPYGLQE YAHVVNAIRF VCDRKSVKHP
     VICSESGRAI VSHHSILIFE AICLTAPATH NEPINIPFIM EGLSEDACAD YWNLRDTAMR
     TGDGAFWFYA DQWKQRCVEQ FKEGTLGIEQ LASVDGLCEW VLKAIGASDP VHTYNINLSV
     FTSIPDLWGI DQLFPIVPIH KLDQRPGARG ILSDLTCDSD GKINKF