ID A0A087HD63_ARAAL Unreviewed; 704 AA.
AC A0A087HD63;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
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};
GN OrderedLocusNames=AALP_Aa3g325600 {ECO:0000313|EMBL:KFK40065.1};
OS Arabis alpina (Alpine rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK40065.1, ECO:0000313|Proteomes:UP000029120};
RN [1] {ECO:0000313|Proteomes:UP000029120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pajares {ECO:0000313|Proteomes:UP000029120};
RX PubMed=27246759; DOI=10.1038/nplants.2014.23;
RA Willing E.M., Rawat V., Mandakova T., Maumus F., James G.V.,
RA Nordstroem K.J., Becker C., Warthmann N., Chica C., Szarzynska B.,
RA Zytnicki M., Albani M.C., Kiefer C., Bergonzi S., Castaings L.,
RA Mateos J.L., Berns M.C., Bujdoso N., Piofczyk T., de Lorenzo L.,
RA Barrero-Sicilia C., Mateos I., Piednoel M., Hagmann J., Chen-Min-Tao R.,
RA Iglesias-Fernandez R., Schuster S.C., Alonso-Blanco C., Roudier F.,
RA Carbonero P., Paz-Ares J., Davis S.J., Pecinka A., Quesneville H.,
RA Colot V., Lysak M.A., Weigel D., Coupland G., Schneeberger K.;
RT "Genome expansion of Arabis alpina linked with retrotransposition and
RT reduced symmetric DNA methylation.";
RL Nat. Plants 1:14023-14023(2015).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM002871; KFK40065.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087HD63; -.
DR EnsemblPlants; KFK40065; KFK40065; AALP_AA3G325600.
DR Gramene; KFK40065; KFK40065; AALP_AA3G325600.
DR eggNOG; ENOG502QTXD; Eukaryota.
DR OMA; MQFEPEL; -.
DR OrthoDB; 305336at2759; -.
DR UniPathway; UPA00186; UER00284.
DR Proteomes; UP000029120; Chromosome 3.
DR GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblPlants.
DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblPlants.
DR GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR GO; GO:0009409; P:response to cold; IEA:EnsemblPlants.
DR GO; GO:0006979; P:response to oxidative stress; IEA:EnsemblPlants.
DR GO; GO:0009651; P:response to salt stress; IEA:EnsemblPlants.
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:SF1; ARGININE DECARBOXYLASE 1-RELATED; 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 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:PIRSR001336-50,
KW ECO:0000256|RuleBase:RU003740};
KW Reference proteome {ECO:0000313|Proteomes:UP000029120};
KW Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066,
KW ECO:0000256|RuleBase:RU003740}.
FT DOMAIN 130..383
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT ACT_SITE 526
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 138
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001336-50"
SQ SEQUENCE 704 AA; 76598 MW; 5156D22DEA389ED4 CRC64;
MPALACVDTT PIVVDTFSSN DCGIYSQFWS PSLSASLYRI DAWGAPYFTT NTSGNISVRP
HGSYTLPNQD IDLLNVVKHV TDPKSTGGLG LGLGLGLPLI VRFPDVLKNR LESLQSSFDF
AIQTQGYDSH YQGVYPVKCN QDRYIIEDIV EFGSSFRFGL EAGSKPEILL AMSCLCKGNL
EAFLVCNGFK DAEYVSLALL GRKLELNTVI VLEQEDELDL VVDLSKKMNI KPVIGLRAKL
RTKHSGHFGS TSGEKGKFGL TTVQIVRVVK KLREKGMLDC LQLLHFHIGS QIPSTALLSD
GVAEAAQLYC ELVRLGACMG VIDIGGGLGI DYDGSKSGES DLSVAYSLEE YAAAVVASVR
FVCDQKSVKH PVICSESGRA IVSHHSVLIF EAVSAGKQHE TPTDIQFLLE GYSEEARGDY
ENLYGAAMRG DRDSCLIYVD QLKQRCVEGF KEGSLSIEQL AGVDGLCESV IKAIGASDPV
LTYNVNLSVF TSIPDFWGID QLFPIVPIHR LDQRPMARGI LSDLTCDSDG KINKFIGGES
SLPLHELDTN GCSNGRYYLG MFLGGAYEEA LGGVHNLFGG PSVVRVLQSD GPHGFEVTRA
VMGQSSADVL RAMQHEPELM FQTLQHRAEE LSKAQRNNKV SAEKLAASCL ARSFNNMPYL
SMETSTNALT AAINNLGVYY RDEAPCDGGK DEKWAYFGGV LKET
//
