ID O81166_BRAOL Unreviewed; 403 AA.
AC O81166;
DT 01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1998, sequence version 1.
DT 08-NOV-2023, entry version 86.
DE RecName: Full=Arginine decarboxylase {ECO:0000256|ARBA:ARBA00012426, ECO:0000256|RuleBase:RU003740};
DE EC=4.1.1.19 {ECO:0000256|ARBA:ARBA00012426, ECO:0000256|RuleBase:RU003740};
DE Flags: Fragment;
GN Name=spe2 {ECO:0000313|EMBL:AAC68517.1};
OS Brassica oleracea (Wild cabbage).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3712 {ECO:0000313|EMBL:AAC68517.1};
RN [1] {ECO:0000313|EMBL:AAC68517.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=9787437;
RA Galloway G.L., Malmberg R.L., Price R.A.;
RT "Phylogenetic utility of the nuclear gene arginine decarboxylase: an
RT example from Brassicaceae.";
RL Mol. Biol. Evol. 15:1312-1320(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 Evidence={ECO:0000256|ARBA:ARBA00000009,
CC ECO:0000256|RuleBase:RU003740};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|RuleBase:RU003740};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR600183-50, ECO:0000256|RuleBase:RU003740};
CC -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC agmatine from L-arginine: step 1/1. {ECO:0000256|ARBA:ARBA00004773,
CC ECO:0000256|RuleBase:RU003740}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC SpeA subfamily. {ECO:0000256|ARBA:ARBA00008357,
CC ECO:0000256|RuleBase:RU003740}.
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DR EMBL; AF045672; AAC68517.1; -; Genomic_DNA.
DR AlphaFoldDB; O81166; -.
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: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; IPR000183; Orn/DAP/Arg_de-COase.
DR InterPro; IPR029066; PLP-binding_barrel.
DR PANTHER; PTHR43295; ARGININE DECARBOXYLASE; 1.
DR PANTHER; PTHR43295:SF1; ARGININE DECARBOXYLASE 1-RELATED; 1.
DR Pfam; PF02784; Orn_Arg_deC_N; 1.
DR PRINTS; PR01180; ARGDCRBXLASE.
DR PRINTS; PR01179; ODADCRBXLASE.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS00879; ODR_DC_2_2; 1.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793,
KW ECO:0000256|RuleBase:RU003740};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003740};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU003740};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50,
KW ECO:0000256|RuleBase:RU003740};
KW Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066,
KW ECO:0000256|RuleBase:RU003740}.
FT DOMAIN 4..253
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT ACT_SITE 394
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 8
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAC68517.1"
FT NON_TER 403
FT /evidence="ECO:0000313|EMBL:AAC68517.1"
SQ SEQUENCE 403 AA; 44283 MW; 6E5F0BE3D32EF768 CRC64;
YQGVYPVKGN QDRFVVEDIV RFGSQFRFGL EAGSKPEILL AMSCLCKGNP DAFLVCNGFK
DAEYIFLALL GRKLALNTVI VLEQEEELDL VIDLSQKMNV RPVIGLRAKL RTKHSGHFGS
TSGEKGKFGL TTTQIVRVMR KLSQSGMLDC LQLLHFHIGS QIPSTSLLSD GVAEAAQLYC
ELVRLGAHMK VIDIGGGLGI DYDGSKSGES DLSVAYTLEE YAEAVVASVR FVCDRRSVKH
PVICSESGRA IVSHHSVLIF EAVSAVKPMA HQANPDDIQF LLEGNEEYED LYAAVMRGDH
ESCLLYVDQL KQRCVEGFKD GVLSIEQLAS VDGLCEWVLK AIGASDPVHT YNINLSVFTS
IPDLWGIEQL FPIVPIHKLD QRPGTRGILS DLTCDSDGKI SKF
//
