UniProt: Q9M617

Database: UniProt
Entry: Q9M617_BRAJU

LinkDB:  Q9M617_BRAJU 
Original site:  Q9M617_BRAJU

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (7)   
   Pfam (1)   
   PROSITE (2)   
Literature (1)   
   PubMed (1)   
All databases (16)   

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ID   Q9M617_BRAJU            Unreviewed;       680 AA.
AC   Q9M617;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   13-SEP-2023, entry version 85.
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};
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 {ECO:0000313|EMBL:AAF26435.1};
RN   [1] {ECO:0000313|EMBL:AAF26435.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12060267; DOI=10.1034/j.1399-3054.2002.1140314.x;
RA   Mo H., Pua E.C.;
RT   "Up-regulation of arginine decarboxylase gene expression and accumulation
RT   of polyamines in mustard (Brassica juncea)in response to stress.";
RL   Physiol. Plantarum 114:439-449(2002).
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:PIRSR001336-50, 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; AF220098; AAF26435.1; -; mRNA.
DR   AlphaFoldDB; Q9M617; -.
DR   BioCyc; MetaCyc:MONOMER-14983; -.
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; IPR022653; De-COase2_pyr-phos_BS.
DR   InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   NCBIfam; TIGR01273; speA; 1.
DR   PANTHER; PTHR43295; ARGININE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43295:SF8; ARGININE DECARBOXYLASE; 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; SSF51419; PLP-binding barrel; 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 {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:PIRSR001336-50,
KW   ECO:0000256|RuleBase:RU003740};
KW   Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066,
KW   ECO:0000256|RuleBase:RU003740}.
FT   DOMAIN          129..379
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   ACT_SITE        516
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         137
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001336-50"
SQ   SEQUENCE   680 AA;  74357 MW;  D08E48557D7A2BE9 CRC64;
     MPALACVDTY TTDVFIPPSP QPSSTAAVVD TWSPSLSSSL YRIDGWGAPY FSANSSGNIS
     VRPHGSNTLP HQDIDLLKLV KKVTDPKQTG GLGLHLPVIV RFPDVLKNRL ECLQSAFDFA
     VQSQGYESHY QGVYPVKCNQ DRFVVEDIVR FGSQFRFGLE AGSKPEILLA MSCLCKGNNE
     AFLICNGFKD AEYVSLALLG RKLALNTVIV LEQEEELDLG IDLSHKMNVR PVIGLRAKLR
     TKHSGHFGST SGEKGKFGLT TTQIVRVVRK LVCLTVSSFL HFHIGSQIPS TSLLSDGVSE
     AAQLYCELVR LGANMKVIDI GGGLGIDYDG SKSGESDLSV AYTLEEYAEA VVASVRFVCE
     RRSVKHPVIC SESGRAIVSH HSVLIFEAVS TVKHQADHDD IQFLLEGDDY EELYSAVMRG
     DQERCLLYVE KLKQRCVEGF KDGVLSIEQL ASVDGLCEWV LKAIGGSDPV QTYNINLSVF
     TSVPDLWGIE QLFPIVPIHK LDQRPGTRGV LSDLTCDSDG KIDKFIGGES TLPLHELESG
     GGRYFLGMFL GGAYEEALGG VHNLFGGPSV VRVLQSDGPH SFAVTRAVPG QSSADVLRGM
     QHEPEMMFET LKHRAEEVMH RKGGEGEDDD EGEFCNVAAC LDRSFHNMPY LATEEVLSMS
     NSLSDAVSNL GFYYCDEDGF
//

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