ID G4V2K8_9BRAS Unreviewed; 361 AA.
AC G4V2K8;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 03-MAY-2023, entry version 35.
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;
OS Smelowskia annua.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Smelowskieae; Smelowskia.
OX NCBI_TaxID=225687 {ECO:0000313|EMBL:ADN93134.1};
RN [1] {ECO:0000313|EMBL:ADN93134.1}
RP NUCLEOTIDE SEQUENCE.
RA Zhao B., Wang J.B.;
RT "Phylogenetic relationships of Brassicaceae from China.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
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|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; GQ982933; ADN93134.1; -; Genomic_DNA.
DR AlphaFoldDB; G4V2K8; -.
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 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; 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.
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|RuleBase:RU003740};
KW Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066,
KW ECO:0000256|RuleBase:RU003740}.
FT DOMAIN 8..214
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADN93134.1"
FT NON_TER 361
FT /evidence="ECO:0000313|EMBL:ADN93134.1"
SQ SEQUENCE 361 AA; 39218 MW; FB618245F92E65B6 CRC64;
LAMSCLCKGN PEAFLVCNGF KDSEYISLAL LGRKLELNTV IVLEQEEELD LVIDLSQKMN
VRPVIGLRAK LRTKHSGHFG STSGEKGKFG LTTSQIVRVV RKLRQVGMLD CLQLLHFHIG
SQIPSTALLS DGVAEAAQLY CELSRLGAHM KVIGIGGGLG IDYDGSKSGE SDLSVAYSLE
EYAAAVVASI RFACDQKSVK HPVICSESGR AIVSHHSVLI FEAVSAGKQH ETPTDVQFLL
EGYSEEARGD YENLYGAAMR GDRESCLLYV DRLKQRCVEG FKEGSLSIEQ LAAVDGLCES
VIKAIGASDP VLTYHVNLSI FTSIPDFWGI DQLFPIVPIH KLDQRPVARG ILSDLTCDSD
G
//
