ID G4V2P1_9BRAS Unreviewed; 362 AA.
AC G4V2P1;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 03-MAY-2023, entry version 36.
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 Chorispora sibirica.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Chorisporeae; Chorispora.
OX NCBI_TaxID=282603 {ECO:0000313|EMBL:ADN93167.1};
RN [1] {ECO:0000313|EMBL:ADN93167.1}
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; GQ982966; ADN93167.1; -; Genomic_DNA.
DR AlphaFoldDB; G4V2P1; -.
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; 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|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:ADN93167.1"
FT NON_TER 362
FT /evidence="ECO:0000313|EMBL:ADN93167.1"
SQ SEQUENCE 362 AA; 39637 MW; 617F65807109D7FE CRC64;
LAMSCFCKGN PDAFLVCNGF KDAEYISLAL LGRKLALNTV IVLEQEEELD LVIDLSQKMN
VRPVIGLRAK LRTKHSGHFG STSGEKGKFG LTTTQIVRVM RKLSQSGMLD CLQLLHFHIG
SQIPSTSLLT DGVAEATQLY CELVRLGAHM EVIDIGGGLG IDYDGSKSGE SDLSVAYTLE
EYAEAVVASI RYVCDRRSVK HPVICSESGR ALVSHHSVLI FEAVSASNPT VHQTSPNDIQ
FLLEAEEARA DYEDLYAAVM RGDHESCLVY VDQLKQRCVE GFKEGVFSIE QLASVNGLCE
WVLKAIGASD PVRTYNINLS VFTSIPDLWG IDQLFPIVPI HKLDQRPGNR GILSDLTCDS
DG
//
