SPE2_ARATH
ID SPE2_ARATH Reviewed; 711 AA.
AC O23141; Q8H165; Q93ZG4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Arginine decarboxylase 2 {ECO:0000305};
DE Short=ADC 2 {ECO:0000305};
DE Short=ARGDC 2 {ECO:0000305};
DE Short=AtADC2 {ECO:0000303|PubMed:14684170};
DE EC=4.1.1.19 {ECO:0000305|PubMed:14684170};
DE AltName: Full=ADC-N {ECO:0000305};
GN Name=ADC2 {ECO:0000303|PubMed:14684170};
GN Synonyms=SPE2 {ECO:0000303|PubMed:9680979};
GN OrderedLocusNames=At4g34710 {ECO:0000312|Araport:AT4G34710};
GN ORFNames=T4L20.290 {ECO:0000312|EMBL:CAA18850.1};
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;
RA Watson M.B., Yu W., Galloway G., Malmberg R.L.;
RT "Isolation and characterization of a second arginine decarboxylase cDNA
RT from Arabidopsis.";
RL (er) Plant Gene Register PGR97-114(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 INDUCTION BY OSMOTIC STRESS.
RX PubMed=10481069; DOI=10.1016/s0014-5793(99)01125-4;
RA Soyka S., Heyer A.G.;
RT "Arabidopsis knockout mutation of ADC2 gene reveals inducibility by osmotic
RT stress.";
RL FEBS Lett. 458:219-223(1999).
RN [7]
RP INDUCTION.
RX PubMed=12428010; DOI=10.1104/pp.009951;
RA Perez-Amador M.A., Leon J., Green P.J., Carbonell J.;
RT "Induction of the arginine decarboxylase ADC2 gene provides evidence for
RT the involvement of polyamines in the wound response in Arabidopsis.";
RL Plant Physiol. 130:1454-1463(2002).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION BY SALT STRESS.
RX PubMed=14684170; DOI=10.1016/j.bbrc.2003.11.119;
RA Urano K., Yoshiba Y., Nanjo T., Ito T., Yamaguchi-Shinozaki K.,
RA Shinozaki K.;
RT "Arabidopsis stress-inducible gene for arginine decarboxylase AtADC2 is
RT required for accumulation of putrescine in salt tolerance.";
RL Biochem. Biophys. Res. Commun. 313:369-375(2004).
RN [9]
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 [10]
RP FUNCTION.
RX PubMed=16045477; DOI=10.1111/j.1365-313x.2005.02465.x;
RA Alcazar R., Garcia-Martinez J.L., Cuevas J.C., Tiburcio A.F., Altabella T.;
RT "Overexpression of ADC2 in Arabidopsis induces dwarfism and late-flowering
RT through GA deficiency.";
RL Plant J. 43:425-436(2005).
RN [11]
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 [12]
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 [13]
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 [14]
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).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=28716421; DOI=10.1016/j.plantsci.2017.05.011;
RA Patel J., Ariyaratne M., Ahmed S., Ge L., Phuntumart V., Kalinoski A.,
RA Morris P.F.;
RT "Dual functioning of plant arginases provides a third route for putrescine
RT synthesis.";
RL Plant Sci. 262:62-73(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:14684170, PubMed:15733873, PubMed:16045477,
CC PubMed:25409942). Is a major contributor to basal arginine
CC decarboxylase (ADC) activity and putrescine biosynthesis
CC (PubMed:25409942). Accumulation of putrescine plays a positive role in
CC salt stress tolerance (PubMed:14684170). Accumulation of putrescine
CC plays a positive role in freezing tolerance (PubMed:18701673).
CC Production of PA 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:14684170, ECO:0000269|PubMed:15733873,
CC ECO:0000269|PubMed:16045477, ECO:0000269|PubMed:18701673,
CC ECO:0000269|PubMed:25409942, 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:0000305|PubMed:14684170};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC agmatine from L-arginine: step 1/1. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer and heterodimer with ADC1.
CC {ECO:0000269|PubMed:28109885}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:28109885, ECO:0000269|PubMed:28716421}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:28109885}. Note=Localizes mainly in the
CC chloroplast. {ECO:0000269|PubMed:28109885}.
CC -!- INDUCTION: Induced by wounding, methyl jasmonate and abscisic acid
CC (ABA) (PubMed:12428010). Induced by salt stress (PubMed:14684170).
CC Induced by osmotic stress (PubMed:10481069). Induced by freezing
CC (PubMed:18701673). Induced by the bacterial pathogen Pseudomonas
CC viridiflava (PubMed:25409942). {ECO:0000269|PubMed:10481069,
CC ECO:0000269|PubMed:12428010, ECO:0000269|PubMed:14684170,
CC ECO:0000269|PubMed:18701673, ECO:0000269|PubMed:25409942}.
CC -!- DISRUPTION PHENOTYPE: Increased levels of lateral root branching.
CC {ECO:0000269|PubMed:9680979}.
CC -!- MISCELLANEOUS: Plants over-expressing ADC2 accumulate very high levels
CC of putrescine and exhibit dwarfism and late-flowering phenotypes.
CC {ECO:0000269|PubMed:16045477}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC SpeA subfamily. {ECO:0000305}.
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DR EMBL; AF009647; AAB72179.1; -; mRNA.
DR EMBL; AL023094; CAA18850.1; -; Genomic_DNA.
DR EMBL; AL161586; CAB80188.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86413.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86414.1; -; Genomic_DNA.
DR EMBL; AY039581; AAK62636.1; -; mRNA.
DR EMBL; AY057553; AAL09792.1; -; mRNA.
DR EMBL; AY093982; AAM16243.1; -; mRNA.
DR EMBL; BT000682; AAN31828.1; -; mRNA.
DR PIR; T05291; T05291.
DR RefSeq; NP_195197.1; NM_119637.3.
DR RefSeq; NP_974684.1; NM_202955.1.
DR AlphaFoldDB; O23141; -.
DR SMR; O23141; -.
DR BioGRID; 14905; 1.
DR IntAct; O23141; 1.
DR STRING; 3702.AT4G34710.1; -.
DR iPTMnet; O23141; -.
DR PaxDb; O23141; -.
DR PRIDE; O23141; -.
DR ProteomicsDB; 245334; -.
DR EnsemblPlants; AT4G34710.1; AT4G34710.1; AT4G34710.
DR EnsemblPlants; AT4G34710.2; AT4G34710.2; AT4G34710.
DR GeneID; 829623; -.
DR Gramene; AT4G34710.1; AT4G34710.1; AT4G34710.
DR Gramene; AT4G34710.2; AT4G34710.2; AT4G34710.
DR KEGG; ath:AT4G34710; -.
DR Araport; AT4G34710; -.
DR TAIR; locus:2139629; AT4G34710.
DR eggNOG; ENOG502QTXD; Eukaryota.
DR HOGENOM; CLU_027243_0_0_1; -.
DR InParanoid; O23141; -.
DR OMA; AVEYTQH; -.
DR OrthoDB; 762520at2759; -.
DR PhylomeDB; O23141; -.
DR BioCyc; ARA:AT4G34710-MON; -.
DR BRENDA; 4.1.1.19; 399.
DR UniPathway; UPA00186; UER00284.
DR PRO; PR:O23141; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23141; baseline and differential.
DR Genevisible; O23141; 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; IMP:TAIR.
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; IMP:TAIR.
DR GO; GO:0033388; P:putrescine biosynthetic process from arginine; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009409; P:response to cold; IMP:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; 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:0009611; P:response to wounding; IEP: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.
FT CHAIN 1..711
FT /note="Arginine decarboxylase 2"
FT /id="PRO_0000149947"
FT REGION 642..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 331..341
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 147
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 54
FT /note="D -> Y (in Ref. 4; AAL09792)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="V -> F (in Ref. 4; AAN31828)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="F -> Y (in Ref. 4; AAN31828)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 711 AA; 77219 MW; 8E003877173DEEE5 CRC64;
MPALACVDTS FVPPAYAFSD TAGDVFIPAS SPTSAAVVVD RWSPSLSSSL YRIDGWGAPY
FIANSSGNIS VRPHGSETLP HQDIDLLKIV KKVTGPKSSG GLGLQLPLIV RFPDVLKNRL
ECLQSAFDYA IKSQGYDSHY QGVYPVKCNQ DRFVVEDIVK FGSSFRFGLE AGSKPEILLA
MSCLCKGSPD AFLVCNGFKD AEYISLALLG RKLALNTVIV LEQEEELDLV IELSQKMNVR
PVIGLRAKLR TKHSGHFGST SGEKGKFGLT TTQIVRVVRK LRQSGMLDCL QLLHFHIGSQ
IPSTSLLSDG VAEAAQLYCE LVRLGAHMKV IDIGGGLGID YDGSKSGESD LSVAYSLEEY
AEAVVASVRV VCDRSSVKHP VICSESGRAI VSHHSVLIFE AVSADKPMVH QATPGDIQFL
LEGNEEARAN YEDLYAAVMR GDHESCLLYV DQLKQRCVEG FKEGVLSIEQ LASVDGLCEW
VLKAIGASDP VHTYNINLSV FTSIPDLWGI DQLFPIVPIH KLDQRPGARG ILSDLTCDSD
GKINKFIGGE SSLPLHELDK NGSGGRYFLG MFLGGAYEEA LGGVHNLFGG PSVVRVSQSD
GPHSFAVTRA VPGQSSADVL RAMQHEPELM FQTLKHRAEE MMHTKGGSEG ENEEEEEDDE
FNNVAASLDR SFHNMPYLAT EQASPSNSLS AAISNLGFYY CDEDVYDYIS A
