ID   SPE1_SOYBN              Reviewed;         692 AA.
AC   Q39827;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-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   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Nam K.H., Lee S.H., Lee J.H.;
RT   "A cDNA encoding an arginine decarboxylase from soybean hypocotyls.";
RL   (er) Plant Gene Register PGR95-142(1995).
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; U35367; AAD09204.1; -; mRNA.
DR   PIR; T06593; T06593.
DR   RefSeq; NP_001238359.1; NM_001251430.1.
DR   AlphaFoldDB; Q39827; -.
DR   SMR; Q39827; -.
DR   STRING; 3847.Q39827; -.
DR   PaxDb; 3847-GLYMA06G00990-2; -.
DR   GeneID; 548071; -.
DR   KEGG; gmx:548071; -.
DR   eggNOG; ENOG502QTXD; Eukaryota.
DR   InParanoid; Q39827; -.
DR   OrthoDB; 305336at2759; -.
DR   BRENDA; 4.1.1.19; 2483.
DR   SABIO-RK; Q39827; -.
DR   UniPathway; UPA00186; UER00284.
DR   Proteomes; UP000008827; Unplaced.
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:SF1; ARGININE DECARBOXYLASE 1-RELATED; 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   2: Evidence at transcript level;
KW   Decarboxylase; Lyase; Magnesium; Putrescine biosynthesis;
KW   Pyridoxal phosphate; Reference proteome; Spermidine biosynthesis.
FT   CHAIN           1..692
FT                   /note="Arginine decarboxylase"
FT                   /id="PRO_0000149954"
FT   BINDING         337..347
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         153
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   692 AA;  74595 MW;  31BA9C207B5A6EF3 CRC64;
     MPVLACCVDA AAPPGYAFAG DISFPAPIAF TGVPPATADD TNNSNNHWSP SLSAALYNVD
     GWGGPYFAVN TAGNISVRPH GSDTVSHQEI DLLKIVKKAS DPKSLGGLSL QLPLIARFPD
     VLKNRLESLQ SAFDYAIQSG GYESHYQGVY PVKCNQDRFV VEDIVKFGSP FRFGLEAGSK
     PELLLAMSCL CKGNPDGLLI CNGFKDAEYI SLALVANKLA LNTVIVVEQE EEVDLIVELS
     KKLCIKPVIG LRAKLRTKHS GHFGGIFRRR GKFGLTTARV LRVVKNLDLA GMLDCLQLLH
     FHIGSQIPST ALLADGVGEA AQIYCELVRL GANMRVIDIG GGLGIDYDGS KSCDSDISVE
     YGLEEYAAAV VHAVQCVCDR SVKHPVICSE SGRAIVSHHS VLIFEAVGTS STNGGGAPPA
     LSAHYLAEEL SEDYGYLSEL AFRGDYETCL VYTEEMKERC VEQFKQGTVC MEQLAAVEGL
     CELVRKAVGA AESVRRYHVN LSIFTSVPDA WGIEQVFPII PIHRLDEKPS VRGILSDLTC
     DSDGKIDKFI NGESSLPLHE MEGGRTYYLG MFLGGAYEEA LGGVHNLFGG PSVVRVSQSD
     GPHSFAVTRA VPGPSCGDVL RVMQHQPELM FETLKHRAQE YVSHDNAAAL LAAGLARTFD
     RMPYLLSLSS FVADDVAAAV PAAQDLGEQW SY
//