SPE1_PEA
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 03-AUG-2022, entry version 91.
DE RecName: Full=Arginine decarboxylase;
DE Short=ADC;
DE Short=ARGDC;
DE EC=4.1.1.19;
OS Pisum sativum (Garden pea).
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; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX 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:
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; Z37540; CAA85773.1; -; mRNA.
DR PIR; S59553; S59553.
DR AlphaFoldDB; Q43075; -.
DR SMR; Q43075; -.
DR EnsemblPlants; Psat7g140360.1; Psat7g140360.1.cds1; Psat7g140360.
DR Gramene; Psat7g140360.1; Psat7g140360.1.cds1; Psat7g140360.
DR BioCyc; MetaCyc:MON-14984; -.
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:0009409; P:response to cold; IEA:EnsemblPlants.
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 PIRSF; PIRSF001336; Arg_decrbxlase; 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; Spermidine biosynthesis.
FT CHAIN 1..728
FT /note="Arginine decarboxylase"
FT /id="PRO_0000149953"
FT BINDING 345..355
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 161
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
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