SPE1_BRAJU
ID SPE1_BRAJU Reviewed; 702 AA.
AC O82475;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Arginine decarboxylase;
DE Short=ADC;
DE Short=ARGDC;
DE EC=4.1.1.19;
GN Name=ADC1;
OS Brassica juncea (Indian mustard) (Sinapis juncea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3707;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Mo H., Pua E.-C.;
RT "Molecular cloning of an arginine decarboxylase cDNA from mustard (Brassica
RT juncea [L.] Czern & Coss).";
RL (er) Plant Gene Register PGR98-160(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; AF077547; AAC62017.1; -; mRNA.
DR AlphaFoldDB; O82475; -.
DR SMR; O82475; -.
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; 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..702
FT /note="Arginine decarboxylase"
FT /id="PRO_0000149949"
FT BINDING 325..335
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 141
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 702 AA; 76188 MW; 4FF22C7A8D1B1B92 CRC64;
MPALALVDTP VDAFSGDCSG VFIPPSPNSS SASLDWSPSL SSSLYRIDGW GAPYFAANSS
GNISVRPHGS NTMPHQEIDL TKVVKKATDP KSSGGLALQF PLIVRFPDVL KNRLESLQSA
FEFAIQTQGY ESRYQGVYPV KCNQDRFIIE DIVEFGSSFR FGLEAGSKPE ILLAMSCLCK
GSPEAFLVCN GFKDAEYVSL ALLGRKLQLN TVIVLEQEEE LDLVIALSKK VNVRPVIGLR
AKLRTKHSGH FGSTSGEKGK FGLTTVQIIR VVRKLRDVGM LDCLQLLHFH IGSQIPSTAL
LSDGVSEAAQ LYCELVRLGA RMEVIDIGGG LGIDYDGSKS GESDLSVAYS LEEYAAAVVA
SVRFVCDQKS VKHPVICSES GRAIVSHHSV LIFEAVSAGK RHETTPSDLQ FLLEGYSEEA
RGDYENLYDA VMRGDRESCL LYVDQLKQRC VEEFKEGSLS IEQLAGVDGL CEWVTKEIGG
SDPVLTYNVN LSVFHSIPDF WGIDQLFPIV PIHRLDQRPV ARGILSDLTC DSDGKINKFI
GGESSLPLHE LDNNGYYLGM FLGGAYEEAL GGVHNLFGGP SVVRVLQKDG PHGFAVTRAM
MGQSSADVLR AMQHEPELMF QTLKHRAEEL SLVHKPGGDK GNDKLVASCL ARSFNNMPYL
SVGTSTNALT AAINNLVYYS DEAAVGNGGG CGKNGKWSYS VD
