ID A2XPL5_ORYSI Unreviewed; 623 AA.
AC A2XPL5;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 24-JAN-2024, entry version 88.
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 Name=Adc2 {ECO:0000313|EMBL:BBC69459.1};
GN ORFNames=OsI_14579 {ECO:0000313|EMBL:EAY92775.1};
OS Oryza sativa subsp. indica (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=39946 {ECO:0000313|EMBL:EAY92775.1, ECO:0000313|Proteomes:UP000007015};
RN [1] {ECO:0000313|EMBL:EAY92775.1, ECO:0000313|Proteomes:UP000007015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11 {ECO:0000313|Proteomes:UP000007015};
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., Chen H., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA Zheng W., Hao B., Liu S., Wang W., Yuan L., Cao M., McDermott J.,
RA Samudrala R., Wang J., Wong G.K., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [2] {ECO:0000313|EMBL:EAY92775.1}
RP NUCLEOTIDE SEQUENCE.
RA Wang J., Li R., Fan W., Huang Q., Zhang J., Zhou Y., Hu Y., Zi S., Li J.,
RA Ni P., Zheng H., Zhang Y., Zhao M., Hao Q., McDermott J., Samudrala R.,
RA Kristiansen K., Wong G.K.-S.;
RT "Improved gene annotation of the rice (Oryza sativa) genomes.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:EAY92775.1}
RP NUCLEOTIDE SEQUENCE.
RA Wang J., Li R., Fan W., Huang Q., Zhang J., Zhou Y., Hu Y., Zi S., Li J.,
RA Ni P., Zheng H., Zhang Y., Zhao M., Hao Q., McDermott J., Samudrala R.,
RA Kristiansen K., Wong G.K.-S.;
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:BBC69459.1}
RP NUCLEOTIDE SEQUENCE.
RA Rangan P.;
RT "Arginine decarboxylase 2 gene.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; LC369125; BBC69459.1; -; Genomic_DNA.
DR EMBL; CM000129; EAY92775.1; -; Genomic_DNA.
DR AlphaFoldDB; A2XPL5; -.
DR SMR; A2XPL5; -.
DR STRING; 39946.A2XPL5; -.
DR EnsemblPlants; BGIOSGA015766-TA; BGIOSGA015766-PA; BGIOSGA015766.
DR Gramene; BGIOSGA015766-TA; BGIOSGA015766-PA; BGIOSGA015766.
DR HOGENOM; CLU_027243_0_0_1; -.
DR OMA; TMVEPLM; -.
DR UniPathway; UPA00186; UER00284.
DR Proteomes; UP000007015; Chromosome 4.
DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
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 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:UP000007015};
KW Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066,
KW ECO:0000256|RuleBase:RU003740}.
FT DOMAIN 97..355
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT ACT_SITE 487
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 109
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001336-50"
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
//
