ID SPE1_ARATH Reviewed; 702 AA. AC Q9SI64; Q38938; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 24-JAN-2024, entry version 149. DE RecName: Full=Arginine decarboxylase 1, chloroplastic {ECO:0000305}; DE Short=ADC 1 {ECO:0000305}; DE Short=ADC-O {ECO:0000305}; DE Short=ARGDC 1 {ECO:0000305}; DE Short=AtADC1 {ECO:0000303|PubMed:15733873}; DE EC=4.1.1.19 {ECO:0000269|PubMed:11576438}; DE Flags: Precursor; GN Name=ADC1 {ECO:0000303|PubMed:11576438}; GN Synonyms=SPE1 {ECO:0000303|PubMed:9680979}; GN OrderedLocusNames=At2g16500 {ECO:0000312|Araport:AT2G16500}; GN ORFNames=F1P15.12 {ECO:0000312|EMBL:AAD26494.1}; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Columbia; RX PubMed=8756495; DOI=10.1104/pp.111.4.1077; RA Watson M.B., Malmberg R.L.; RT "Regulation of Arabidopsis thaliana (L.) Heynh Arginine decarboxylase by RT potassium deficiency stress."; RL Plant Physiol. 111:1077-1083(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617197; DOI=10.1038/45471; RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."; RL Nature 402:761-768(1999). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP DISRUPTION PHENOTYPE. RX PubMed=9680979; DOI=10.1046/j.1365-313x.1998.00027.x; RA Watson M.B., Emory K.K., Piatak R.M., Malmberg R.L.; RT "Arginine decarboxylase (polyamine synthesis) mutants of Arabidopsis RT thaliana exhibit altered root growth."; RL Plant J. 13:231-239(1998). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF LYS-136 AND RP CYS-524. RX PubMed=11576438; DOI=10.1046/j.1365-313x.2001.01100.x; RA Hanfrey C., Sommer S., Mayer M.J., Burtin D., Michael A.J.; RT "Arabidopsis polyamine biosynthesis: absence of ornithine decarboxylase and RT the mechanism of arginine decarboxylase activity."; RL Plant J. 27:551-560(2001). RN [7] RP FUNCTION. RX PubMed=15733873; DOI=10.1016/j.febslet.2005.01.048; RA Urano K., Hobo T., Shinozaki K.; RT "Arabidopsis ADC genes involved in polyamine biosynthesis are essential for RT seed development."; RL FEBS Lett. 579:1557-1564(2005). RN [8] RP FUNCTION, AND INDUCTION BY FREEZING. RX PubMed=18701673; DOI=10.1104/pp.108.122945; RA Cuevas J.C., Lopez-Cobollo R., Alcazar R., Zarza X., Koncz C., RA Altabella T., Salinas J., Tiburcio A.F., Ferrando A.; RT "Putrescine is involved in Arabidopsis freezing tolerance and cold RT acclimation by regulating abscisic acid levels in response to low RT temperature."; RL Plant Physiol. 148:1094-1105(2008). RN [9] RP FUNCTION, AND INDUCTION BY BACTERIAL PATHOGEN. RX PubMed=25409942; DOI=10.1111/plb.12289; RA Rossi F.R., Marina M., Pieckenstain F.L.; RT "Role of Arginine decarboxylase (ADC) in Arabidopsis thaliana defence RT against the pathogenic bacterium Pseudomonas viridiflava."; RL Plant Biol. 17:831-839(2015). RN [10] RP FUNCTION. RX PubMed=27014322; DOI=10.3389/fpls.2016.00300; RA Sanchez-Rangel D., Chavez-Martinez A.I., Rodriguez-Hernandez A.A., RA Maruri-Lopez I., Urano K., Shinozaki K., Jimenez-Bremont J.F.; RT "Simultaneous silencing of two arginine decarboxylase genes alters RT development in Arabidopsis."; RL Front. Plant Sci. 7:300-300(2016). RN [11] RP SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=28109885; DOI=10.1016/j.bbrc.2017.01.083; RA Maruri-Lopez I., Jimenez-Bremont J.F.; RT "Hetero- and homodimerization of Arabidopsis thaliana arginine RT decarboxylase AtADC1 and AtADC2."; RL Biochem. Biophys. Res. Commun. 484:508-513(2017). CC -!- FUNCTION: Required for the biosynthesis of putrescine. Catalyzes the CC first step of polyamine (PA) biosynthesis to produce putrescine from CC arginine (PubMed:11576438, PubMed:15733873, PubMed:25409942). Is a CC minor contributor to basal arginine decarboxylase (ADC) activity and CC putrescine biosynthesis (PubMed:25409942). Accumulation of putrescine CC plays a positive role in freezing tolerance (PubMed:18701673). CC Production of polyamines is essential for normal seed development CC (PubMed:15733873). Controls PA homeostasis which is crucial for normal CC plant growth and development (PubMed:27014322). CC {ECO:0000269|PubMed:11576438, ECO:0000269|PubMed:15733873, CC ECO:0000269|PubMed:18701673, ECO:0000269|PubMed:25409942, CC ECO:0000269|PubMed:27014322}. 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:0000269|PubMed:11576438}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250|UniProtKB:P11926}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P21170}; CC -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis; CC agmatine from L-arginine: step 1/1. {ECO:0000305}. CC -!- SUBUNIT: Homodimer. Only the dimer is catalytically active, as the CC active sites are constructed of residues from both monomers. May form a CC head-to-tail homodimer (PubMed:11576438). Homodimer and heterodimer CC with ADC2 (PubMed:28109885). {ECO:0000269|PubMed:11576438, CC ECO:0000269|PubMed:28109885}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast CC {ECO:0000269|PubMed:28109885}. Cytoplasm, cytosol CC {ECO:0000269|PubMed:28109885}. Note=Localizes mainly in the CC chloroplast. {ECO:0000269|PubMed:28109885}. CC -!- INDUCTION: Induced by freezing (PubMed:18701673). Induced by the CC bacterial pathogen Pseudomonas viridiflava (PubMed:25409942). CC {ECO:0000269|PubMed:18701673, ECO:0000269|PubMed:25409942}. CC -!- DISRUPTION PHENOTYPE: Increased levels of lateral root branching. CC {ECO:0000269|PubMed:9680979}. CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family. CC SpeA subfamily. {ECO:0000305}. 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; U52851; AAB09723.1; -; mRNA. DR EMBL; AC007195; AAD26494.1; -; Genomic_DNA. DR EMBL; CP002685; AEC06503.1; -; Genomic_DNA. DR EMBL; BT008636; AAP40453.1; -; mRNA. DR PIR; A84541; A84541. DR PIR; S71239; S71239. DR RefSeq; NP_179243.1; NM_127204.3. DR AlphaFoldDB; Q9SI64; -. DR SMR; Q9SI64; -. DR STRING; 3702.Q9SI64; -. DR PaxDb; 3702-AT2G16500-1; -. DR ProteomicsDB; 232568; -. DR EnsemblPlants; AT2G16500.1; AT2G16500.1; AT2G16500. DR GeneID; 816149; -. DR Gramene; AT2G16500.1; AT2G16500.1; AT2G16500. DR KEGG; ath:AT2G16500; -. DR Araport; AT2G16500; -. DR TAIR; AT2G16500; ADC1. DR eggNOG; ENOG502QTXD; Eukaryota. DR HOGENOM; CLU_027243_0_0_1; -. DR InParanoid; Q9SI64; -. DR OMA; MQFEPEL; -. DR OrthoDB; 305336at2759; -. DR PhylomeDB; Q9SI64; -. DR BioCyc; ARA:AT2G16500-MONOMER; -. DR BRENDA; 4.1.1.19; 399. DR UniPathway; UPA00186; UER00284. DR PRO; PR:Q9SI64; -. DR Proteomes; UP000006548; Chromosome 2. DR ExpressionAtlas; Q9SI64; baseline and differential. DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB. DR GO; GO:0006527; P:arginine catabolic process; IEA:InterPro. DR GO; GO:0006596; P:polyamine biosynthetic process; IMP:TAIR. DR GO; GO:0009446; P:putrescine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009409; P:response to cold; IMP:TAIR. DR GO; GO:0006979; P:response to oxidative stress; IEP:TAIR. DR GO; GO:0009651; P:response to salt stress; IMP:TAIR. 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. DR Genevisible; Q9SI64; AT. PE 1: Evidence at protein level; KW Chloroplast; Cytoplasm; Decarboxylase; Lyase; Magnesium; Plastid; KW Putrescine biosynthesis; Pyridoxal phosphate; Reference proteome; KW Spermidine biosynthesis; Stress response; Transit peptide. FT TRANSIT 1..52 FT /note="Chloroplast" FT /evidence="ECO:0000255" FT CHAIN 53..702 FT /note="Arginine decarboxylase 1, chloroplastic" FT /id="PRO_0000149946" FT ACT_SITE 524 FT /note="Proton donor; shared with dimeric partner" FT /evidence="ECO:0000250|UniProtKB:P11926" FT BINDING 288 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000250|UniProtKB:P11926" FT BINDING 320..330 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 325 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000250|UniProtKB:P11926" FT BINDING 374..377 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000250|UniProtKB:P11926" FT BINDING 436..437 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P07805" FT BINDING 525 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P07805" FT BINDING 565 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000250|UniProtKB:P11926" FT SITE 285 FT /note="Stacks against the aromatic ring of pyridoxal FT phosphate and stabilizes reaction intermediates" FT /evidence="ECO:0000250|UniProtKB:P00860" FT MOD_RES 136 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000250|UniProtKB:P11926" FT MUTAGEN 136 FT /note="K->A: Loss of decarboxylase activity." FT /evidence="ECO:0000269|PubMed:11576438" FT MUTAGEN 524 FT /note="C->A: Loss of decarboxylase activity." FT /evidence="ECO:0000269|PubMed:11576438" FT CONFLICT 452 FT /note="S -> F (in Ref. 1; AAB09723)" FT /evidence="ECO:0000305" SQ SEQUENCE 702 AA; 76175 MW; 8B9D182B2684BCA0 CRC64; MPALAFVDTP IDTFSSIFTP SSVSTAVVDG SCHWSPSLSS SLYRIDGWGA PYFAANSSGN ISVRPHGSNT LPHQDIDLMK VVKKVTDPSG LGLQLPLIVR FPDVLKNRLE CLQSAFDYAI QSQGYDSHYQ GVYPVKCNQD RFIIEDIVEF GSGFRFGLEA GSKPEILLAM SCLCKGNPEA FLVCNGFKDS EYISLALFGR KLELNTVIVL EQEEELDLVI DLSQKMNVRP VIGLRAKLRT KHSGHFGSTS GEKGKFGLTT VQILRVVRKL SQVGMLDCLQ LLHFHIGSQI PSTALLSDGV AEAAQLYCEL VRLGAHMKVI DIGGGLGIDY DGSKSGESDL SVAYSLEEYA AAVVASVRFV CDQKSVKHPV ICSESGRAIV SHHSVLIFEA VSAGQQHETP TDHQFMLEGY SEEVRGDYEN LYGAAMRGDR ESCLLYVDQL KQRCVEGFKE GSLGIEQLAG VDGLCEWVIK AIGASDPVLT YHVNLSVFTS IPDFWGIDQL FPIVPIHKLD QRPAARGILS DLTCDSDGKI NKFIGGESSL PLHEMDNNGC SGGRYYLGMF LGGAYEEALG GVHNLFGGPS VVRVLQSDGP HGFAVTRAVM GQSSADVLRA MQHEPELMFQ TLKHRAEEPR NNNNKACGDK GNDKLVVASC LAKSFNNMPY LSMETSTNAL TAAVNNLGVY YCDEAAAGGG GKGKDENWSY FG //