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Database: UniProt
Entry: ADC2_ORYSJ
LinkDB: ADC2_ORYSJ
Original site: ADC2_ORYSJ 
ID   ADC2_ORYSJ              Reviewed;         623 AA.
AC   Q7XRA1; A0A0P0W684; C0LN13;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   24-JAN-2024, entry version 119.
DE   RecName: Full=Arginine decarboxylase 2;
DE            Short=ARGDC2;
DE            Short=OsADC2;
DE            EC=4.1.1.19;
GN   Name=ADC2; OrderedLocusNames=Os04g0107600, LOC_Os04g01690;
GN   ORFNames=OsJ_13525, OSJNBb0085F13.14;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Eyi 105;
RX   PubMed=20082138; DOI=10.1007/s11248-009-9354-0;
RA   Peremarti A., Bassie L., Zhu C., Christou P., Capell T.;
RT   "Molecular characterization of the Arginine decarboxylase gene family in
RT   rice.";
RL   Transgenic Res. 19:785-797(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447439; DOI=10.1038/nature01183;
RA   Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA   Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA   Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA   Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA   Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA   Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA   Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA   Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA   Li J., Hong G., Xue Y., Han B.;
RT   "Sequence and analysis of rice chromosome 4.";
RL   Nature 420:316-320(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC       agmatine from L-arginine: step 1/1.
CC   -!- TISSUE SPECIFICITY: Expressed in stems (at protein level).
CC       {ECO:0000269|PubMed:20082138}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       SpeA subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACN65507.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR   EMBL; FJ746894; ACN65507.1; ALT_SEQ; mRNA.
DR   EMBL; AL606620; CAE02767.2; -; Genomic_DNA.
DR   EMBL; AP008210; BAF13932.1; -; Genomic_DNA.
DR   EMBL; AP014960; BAS87548.1; -; Genomic_DNA.
DR   EMBL; CM000141; EAZ29450.1; -; Genomic_DNA.
DR   EMBL; AK058573; BAG86737.1; -; mRNA.
DR   EMBL; AK121110; BAH00321.1; -; mRNA.
DR   RefSeq; XP_015633833.1; XM_015778347.1.
DR   RefSeq; XP_015633834.1; XM_015778348.1.
DR   AlphaFoldDB; Q7XRA1; -.
DR   SMR; Q7XRA1; -.
DR   STRING; 39947.Q7XRA1; -.
DR   PaxDb; 39947-Q7XRA1; -.
DR   EnsemblPlants; Os04t0107600-01; Os04t0107600-01; Os04g0107600.
DR   EnsemblPlants; Os04t0107600-02; Os04t0107600-02; Os04g0107600.
DR   GeneID; 4334917; -.
DR   Gramene; Os04t0107600-01; Os04t0107600-01; Os04g0107600.
DR   Gramene; Os04t0107600-02; Os04t0107600-02; Os04g0107600.
DR   KEGG; osa:4334917; -.
DR   eggNOG; ENOG502QTXD; Eukaryota.
DR   HOGENOM; CLU_027243_0_0_1; -.
DR   InParanoid; Q7XRA1; -.
DR   OrthoDB; 348033at2759; -.
DR   PlantReactome; R-OSA-1119304; Putrescine biosynthesis II.
DR   PlantReactome; R-OSA-1119447; Putrescine biosynthesis I.
DR   UniPathway; UPA00186; UER00284.
DR   Proteomes; UP000000763; Chromosome 4.
DR   Proteomes; UP000007752; Chromosome 4.
DR   Proteomes; UP000059680; Chromosome 4.
DR   Genevisible; Q7XRA1; OS.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR   GO; GO:0009446; P:putrescine biosynthetic process; IEA:UniProtKB-KW.
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:SF2; ARGININE DECARBOXYLASE 2; 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; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
DR   PROSITE; PS00878; ODR_DC_2_1; 1.
DR   PROSITE; PS00879; ODR_DC_2_2; 1.
PE   1: Evidence at protein level;
KW   Decarboxylase; Lyase; Magnesium; Putrescine biosynthesis;
KW   Pyridoxal phosphate; Reference proteome; Spermidine biosynthesis.
FT   CHAIN           1..623
FT                   /note="Arginine decarboxylase 2"
FT                   /id="PRO_0000392206"
FT   BINDING         295..305
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         109
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   623 AA;  67335 MW;  A4980874AE0FBA87 CRC64;
     MAKKNYGQVY NILGWGDPYF TVNSHGHLAV KPHGRDTMSG QDIDVHSVIH RALATTITTN
     DGDKKPQFPM ILRFPDVLKN RLDSLHAAFH GAVDSTGYAS RYQGVFPIKV NQNKAVVQDL
     VTFGHGYSYG LEAGSKPELL IAMSCLAKAK PGAYLVCNGY KDADYVALAL SARAMGLNAI
     IVLEMEEELD IVVEQSARLG VEPVIGVRAK LLTKIPGHFG STAGKHGKFG MLADKIYEVA
     GKLKKMGKLH WLKLLHYHVG SMIPTTDIVY NAAAEAAGIY CALVKEHGAT GMTTLDCGGG
     LGVDYDGTRS GSSDMSVAYG LEQYASSIVQ AVRLTCDDNG VPHPVLCTES GRAMASHHSM
     IILEALSAIP EPQDEEDTHH RLLSKIQDLS SKQPRTAHTV NGGGGVDAMH SHAVELKKHG
     IEMYKLAKKL SKRVTGDANG IYNYHMNLSV FSLVPDFWGI GQLFPMMPVS RLNEKPTING
     TLVDITCDSD GKVEKFIRDA VTLPLHPLDD AAAEHGGYYV AALLSGAYQE ALACKHNLFS
     GPTLVRVESA GGGGAFKIVS VELGPTAEEV IGTMRYDVKN DISDVIEKVA TENGVWPMVE
     PLMKKGLTTM PYLNDYKPPK TTF
//
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