SPE1_AVESA
ID SPE1_AVESA Reviewed; 607 AA.
AC P22220;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Arginine decarboxylase;
DE Short=ADC;
DE Short=ARGDC;
DE EC=4.1.1.19;
GN Name=SPE1;
OS Avena sativa (Oat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Poodae; Poeae; Aveninae; Avena.
OX NCBI_TaxID=4498;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 427-437.
RC TISSUE=Leaf;
RX PubMed=2266946; DOI=10.1007/bf00262438;
RA Bell E., Malmberg R.L.;
RT "Analysis of a cDNA encoding arginine decarboxylase from oat reveals
RT similarity to the Escherichia coli arginine decarboxylase and evidence of
RT protein processing.";
RL Mol. Gen. Genet. 224:431-436(1990).
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; X56802; CAA40137.1; -; mRNA.
DR PIR; S12265; S12265.
DR AlphaFoldDB; P22220; -.
DR SMR; P22220; -.
DR BioCyc; MetaCyc:MON-14981; -.
DR BRENDA; 4.1.1.19; 588.
DR SABIO-RK; P22220; -.
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; -; 2.
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 PROSITE; PS00878; ODR_DC_2_1; 1.
DR PROSITE; PS00879; ODR_DC_2_2; 1.
PE 1: Evidence at protein level;
KW Decarboxylase; Direct protein sequencing; Lyase; Magnesium;
KW Putrescine biosynthesis; Pyridoxal phosphate; Spermidine biosynthesis.
FT CHAIN 1..607
FT /note="Arginine decarboxylase"
FT /id="PRO_0000149948"
FT BINDING 290..300
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 104
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 607 AA; 66706 MW; 757114B2C02EF8A5 CRC64;
MAKNYGDVYH VEGWGEPYFA VNKDGHLCVR IYGRETLPGQ EIDVLSVIEQ ATSADGTGKK
LQFPMILRFP DVLRHRINSL HTAFANAIKY TQYGSVYQGV FPVKVNQHKD VVQDMVHFGY
DHSYGLEAGS KPELLIAMSC LTKAKPGAYL VCNGYKDSAY VALALAARAM GLNVIIVLEM
EEELDIVIEE SSKLGVEPVI GVRAKLLTKI PGHFGSTAGK HGKFGLPAEK IYEVAKKLKA
LNKLHWLKLL HFHVGSMIPT TDIVFKAASE ASDIYCALVK EYGVETMTTL DCGGGLGVDY
DGTRSGSSDM SVAYGLEEYA SSIVQAVRLK CDYHGVPHPV LCTESGRAMA SYHSMIILEA
LSAIPEPKDD EDEATTEQLH GRIRDLSSKL QPTGLSMSSH AVHIKKHGIE MYKLGKKLSK
SVTTDAHTIY NYHMNLSVFS LMPDYWGIQH LFPMMPVSRL DEKPTHKATL VDVTCDSDGK
VDKFIRDTET MPLHPLDPKL GGYYVAVLLT GAYQEALSNK HNLFGGPSLV RVVGTGNGGA
FNVEAALLGS TTEELIGTVS YDVKQDISSV IEERARENKV WEMVEKLVES GLHTMPYLAD
YKPPPMA
