SPE1_ARATH
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 03-AUG-2022, entry version 142.
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}.
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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.AT2G16500.1; -.
DR PaxDb; Q9SI64; -.
DR PRIDE; Q9SI64; -.
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; locus:2045111; AT2G16500.
DR eggNOG; ENOG502QTXD; Eukaryota.
DR HOGENOM; CLU_027243_0_0_1; -.
DR InParanoid; Q9SI64; -.
DR OMA; TRAVMGQ; -.
DR OrthoDB; 762520at2759; -.
DR PhylomeDB; Q9SI64; -.
DR BioCyc; ARA:AT2G16500-MON; -.
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 Genevisible; Q9SI64; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0008792; F:arginine decarboxylase activity; IBA:GO_Central.
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:0033388; P:putrescine biosynthetic process from arginine; IBA:GO_Central.
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; 2.40.37.10; -; 1.
DR Gene3D; 3.20.20.10; -; 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 PANTHER; PTHR43295; PTHR43295; 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; SSF51419; 1.
DR TIGRFAMs; TIGR01273; speA; 1.
DR PROSITE; PS00878; ODR_DC_2_1; 1.
DR PROSITE; PS00879; ODR_DC_2_2; 1.
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
