ADC1A_TOBAC
ID ADC1A_TOBAC Reviewed; 733 AA.
AC A0A1S3YCW2; Q76BK9;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Arginine decarboxylase 1A, chloroplastic {ECO:0000303|PubMed:32242247};
DE EC=4.1.1.19 {ECO:0000250|UniProtKB:Q9SI64};
DE Flags: Precursor;
GN Name=ADC1A {ECO:0000303|PubMed:32242247}; Synonyms=ADC {ECO:0000303|Ref.1};
GN ORFNames=LOC107774919 {ECO:0000312|RefSeq:XP_016450076.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH TMV REPLICASE.
RC STRAIN=cv. Xanthi; TISSUE=Leaf;
RX DOI=10.1007/s10327-004-0139-2;
RA Shimizu T., Yamaji Y., Ogasawara Y., Hamada K., Sakurai K., Kobayashi T.,
RA Watanabe T., Hibi T.;
RT "Interaction between the helicase domain of the tobacco mosaic virus
RT replicase and a tobacco arginine decarboxylase.";
RL J. Gen. Plant Pathol. 70:353-358(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90;
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=cv. K326-ALCS3;
RX PubMed=32242247; DOI=10.1007/s00425-020-03387-1;
RA Hidalgo Martinez D., Payyavula R.S., Kudithipudi C., Shen Y., Xu D.,
RA Warek U., Strickland J.A., Melis A.;
RT "Genetic attenuation of alkaloids and nicotine content in tobacco
RT (Nicotiana tabacum).";
RL Planta 251:92-92(2020).
CC -!- FUNCTION: Involved in the biosynthesis of pyridine alkaloid natural
CC products, leading mainly to the production of anabasine, anatabine,
CC nicotine and nornicotine, effective deterrents against herbivores with
CC antiparasitic and pesticide properties (neurotoxins); nornicotine
CC serves as the precursor in the synthesis of the carcinogen compound N'-
CC nitrosonornicotine (NNN) (PubMed:32242247). Required for the
CC biosynthesis of putrescine (By similarity). Catalyzes the first step of
CC polyamine (PA) biosynthesis to produce putrescine from arginine (By
CC similarity). {ECO:0000250|UniProtKB:Q9SI64,
CC ECO:0000269|PubMed:32242247}.
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:0000250|UniProtKB:Q9SI64};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P21170};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P11926};
CC -!- PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis.
CC {ECO:0000269|PubMed:32242247}.
CC -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC agmatine from L-arginine: step 1/1. {ECO:0000250|UniProtKB:Q9SI64}.
CC -!- SUBUNIT: Interacts, via its C-terminal internal region, with the
CC tobacco mosaic virus (TMV) replicase helicase region.
CC {ECO:0000269|Ref.1}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Reduced alkaloids and nicotin levels associated
CC with a lower putrescine production (PubMed:32242247). Occasionally, an
CC early senescence and a lower viability of the older leaves is observed
CC (PubMed:32242247). {ECO:0000269|PubMed:32242247}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC SpeA subfamily. {ECO:0000305}.
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DR EMBL; AB110952; BAD06581.1; -; mRNA.
DR RefSeq; NP_001312119.1; NM_001325190.1.
DR RefSeq; XP_016450076.1; XM_016594590.1.
DR SMR; A0A1S3YCW2; -.
DR STRING; 4097.A0A1S3YCW2; -.
DR GeneID; 107774919; -.
DR KEGG; nta:107774919; -.
DR OMA; CCVESAV; -.
DR OrthoDB; 762520at2759; -.
DR UniPathway; UPA00107; -.
DR UniPathway; UPA00186; UER00284.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0008792; F:arginine decarboxylase activity; IBA:GO_Central.
DR GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR GO; GO:0033388; P:putrescine biosynthetic process from arginine; IBA:GO_Central.
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 Alkaloid metabolism; Chloroplast; Decarboxylase; Lyase; Magnesium; Plastid;
KW Pyridoxal phosphate; Reference proteome; Spermidine biosynthesis;
KW Transit peptide.
FT TRANSIT 1..44
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 45..733
FT /note="Arginine decarboxylase 1A, chloroplastic"
FT /id="PRO_0000455779"
FT ACT_SITE 548
FT /note="Proton donor; shared with dimeric partner"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 309
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 346
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 395..398
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 460..461
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07805"
FT BINDING 549
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P07805"
FT BINDING 592
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT SITE 306
FT /note="Stacks against the aromatic ring of pyridoxal
FT phosphate and stabilizes reaction intermediates"
FT /evidence="ECO:0000250|UniProtKB:P00860"
FT MOD_RES 157
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT CONFLICT 22
FT /note="W -> G (in Ref. 1; BAD06581)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 733 AA; 79045 MW; D35973D241392D6D CRC64;
MPALGCCVDA AVSPPPGYSF LWDSSLPAPE IFPSGVPPST NTAVATTTTT HWSPAHSSAL
YSIDGWGAPY FTVNSSGDIS VKPHGTDTLP HQEIDLLKVV KKASDPKNLG GLGLQFPLVV
RFPDILKNRL ESLQSVFDYA VQSQGYEAHY QGVYPVKCNQ DRFVVEDIVK FGSGFRFGLE
AGSKPELLLA MSCLCKGSHE GLLVCNGFKD AEYISLALVA RKLMLNTVIV LEQEEELDLV
IDISKKMAVR PVIGLRAKLR TKHSGHFGST SGEKGKFGLT TTQIVRVVKK LEESGMLDCL
QLLHFHIGSQ IPSTALLADG VGEAAQIYCE LVRLGAGMKY IDCGGGLGID YDGTKSCDSD
CSVGYGLQEY ASTVVQAVRF VCDRKNVKHP VICSESGRAI VSHHSVLIFE AVSSTTTRSQ
ELSSVDLQSF VEKLNDDARA DYRNLSAAAI RGEYDTCVLY ADQLKQRCVE QFKDGDLDIE
QLAAVDGICD FVSKAIGASD PVRTYHVNLS IFTSVPDFWA IDQLFPIVPI HKLDERPVVR
GILSDLTCDS DGKIDKFIGG ESSLPLHELG SNGGGGGDGG KYYLGMFLGG AYEEALGGLH
NLFGGPSVLR VSQSDSPHSF AVTCAVPGPS CADVLRAMQH EPELMFETLK HRAEEFVHND
DEQEEDKGLA FASLASSLAQ SFNNMPYLVT NSSCCLTAAA NNGGYYYCND ENIVGVGAES
AAAEEELWPY CVA
