ADC1B_TOBAC
ID ADC1B_TOBAC Reviewed; 730 AA.
AC A0A1S3WYR7;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Arginine decarboxylase 1B, chloroplastic {ECO:0000303|PubMed:32242247};
DE EC=4.1.1.19 {ECO:0000250|UniProtKB:Q9SI64};
DE Flags: Precursor;
GN Name=ADC1B {ECO:0000303|PubMed:32242247};
GN ORFNames=LOC107759371 {ECO:0000312|RefSeq:XP_016432787.1};
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 [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 [2]
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 -!- 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 RefSeq; XP_016432787.1; XM_016577301.1.
DR SMR; A0A1S3WYR7; -.
DR STRING; 4097.A0A1S3WYR7; -.
DR GeneID; 107759371; -.
DR KEGG; nta:107759371; -.
DR OMA; TRAVMGQ; -.
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 3: Inferred from homology;
KW Alkaloid metabolism; Chloroplast; Decarboxylase; Lyase; Magnesium; Plastid;
KW Pyridoxal phosphate; Reference proteome; Spermidine biosynthesis;
KW Transit peptide.
FT TRANSIT 1..37
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 38..730
FT /note="Arginine decarboxylase 1B, chloroplastic"
FT /id="PRO_0000455780"
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 590
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"
SQ SEQUENCE 730 AA; 78886 MW; BD8024BDCB063BCA CRC64;
MPALGCCVDA AVSPPPGYSF LWDSSLPAPE IFPSGVPLST NTAATTTTTT HWSPAHSSAL
YSIDGWGAPY FTVNSSGDIS VKPHGTETLP HQEIDLLKVV KKASDPKNSG GLGLQFPLVV
RFPDILKNRL ESLQSAFDYA VQSQGYEAHY QGVYPVKCNQ DRFVVEDIVK FGSGFRFGLE
AGSKPELLLA MSCLCKGSRE GLLVCNGFKD ADYISLALVA RKLMLNTVIV LEQEEELDLV
IDISRKMAVR PLIGLRAKLR TKHSGHFGST SGEKGKFGLT TTQIVRVVKK LEESGMLDCL
QLLHFHIGSQ IPSTALLADG VGEAAQIYCE LVRLGAGMKY IDCGGGLGID YDGTKSCDSD
CSVGYGLQEY ASTVVQAVRF VCDRKNVKHP VICSESGRAI VSHHSVLIFE AVSSTTTRSQ
ELSSVDLQSF VEKLNDDARA DYRNLSAAAI RGEYDTCVLY ADQLKQRCVE QFKDGNLDIE
QLAAVDGICD FVSKAIGASD PVRTYHVNLS IFTSIPDFWA IDQLFPIVPI HKLDERPGVR
GILSDLTCDS DGKIDKFIGG ESSLPLHELG SNGGGDGGKY YLGMFLGGAY EEALGGLHNL
FGGPSVLRVS QSDSPHSFAV TCAVPGPSCA DVLRAMQHEP ELMFETLKHR AEEFVHNDDE
QEEDKGLAFA SLASSLAQSF NNMPYLVTNS SCCLTATNNG GYYYCNDENI VGVGAESAAA
EEELWPYCVA
