ID   SPE1_PEA                Reviewed;         728 AA.
AC   Q43075;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 51.
DE   RecName: Full=Arginine decarboxylase;
DE            Short=ARGDC;
DE            Short=ADC;
DE            EC=4.1.1.19;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96011747; PubMed=7548836; DOI=10.1007/BF00032662;
RA   Perez-Amador M.A., Carbonell J., Granell A.;
RT   "Expression of arginine decarboxylase is induced during early fruit
RT   development and in young tissues of Pisum sativum (L.).";
RL   Plant Mol. Biol. 28:997-1009(1995).
CC   -!- CATALYTIC ACTIVITY: L-arginine = agmatine + CO(2).
CC   -!- COFACTOR: Pyridoxal phosphate.
CC   -!- COFACTOR: Magnesium.
CC   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADC
CC       pathway; agmatine from L-arginine: step 1/1.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II
CC       family. SpeA subfamily.
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DR   EMBL; Z37540; CAA85773.1; -; mRNA.
DR   PIR; S59553; S59553.
DR   BRENDA; 4.1.1.19; 287.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IEA:EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
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   InterPro; IPR002985; Arg_decrbxlase.
DR   InterPro; IPR000183; De-COase2.
DR   PANTHER; PTHR11482:SF3; Arg_decrbxlase; 1.
DR   Pfam; PF02784; Orn_Arg_deC_N; 1.
DR   Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR   PIRSF; PIRSF001336; Arg_decrbxlase; 1.
DR   PRINTS; PR01180; ARGDCRBXLASE.
DR   PRINTS; PR01179; ODADCRBXLASE.
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; Spermidine biosynthesis.
FT   CHAIN         1    728       Arginine decarboxylase.
FT                                /FTId=PRO_0000149953.
FT   REGION      345    355       Substrate-binding (By similarity).
FT   MOD_RES     161    161       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   728 AA;  78710 MW;  4193A30AEAD8EC4C CRC64;
     MPALTCFVDG AAALLHPPGY ALAGDFTLPL PFTFSAAATI TDDADATAVE DSNSIWSPSL
     SSKLFRIDGW GFPYFGVNAA GDISVRPHGS ATMSHQEIDL LKVVKKASDP KCCGGLGLQL
     PLVVRFPDVL KDRLESIHAA FDGAIQLQGY ESHYQGVYPV KCNQDRYIVE DIVEFGSSFR
     FGLEAGSKPE LLLAMSCLCK GNREAFLVCN GFKDSEYISL ALIARKLALN TVIVLEQEEE
     LDMVVEISNK LCIRPVIGVR AKLKTKHSGH FGATSGDKGK FGLTTIQILH VVKKLEQLDM
     LDCLQLLHFH IGSQIPTTEL LADGVREASQ IYCELLRLGA QMKVLDIGGG LGIDYDGSKS
     GDSDESVAYG LEEYAAAVVH AVKYVCDRKN VKHPVICSES GRAIVSHHSI LIFEASGAST
     NTAPSLSSIE LQYLGEGLSE EALADYQNIS AATLRGEYEA CLLYTEQFKK RCVEEFKQGT
     LGIEQLAAVD GLCDLITETI GVKDPVKKYH VNLSVFTSVP DFWGINQLFP IVPIHRLDEK
     PTARGILSDL TCDSDGKIDK FIGGESSLPL HEMEGHGGGY YLGMFLGGSY EEALGGLHNL
     FGGPSVVRVL QSDGPHGFAV TRAVAGSSCA DVLRVMQHEP QLMFETLKHR ALEFCGQHDD
     DSVVNAGVLA NSLAQSFDNM PYLVSSTTCC LNALTNNNGF YYCSGDDFSA DTVSVATSVA
     GEDENWSY
//