ODC_NICGL
ID ODC_NICGL Reviewed; 433 AA.
AC E0WN94;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Ornithine decarboxylase, chloroplastic {ECO:0000303|PubMed:21232776};
DE EC=4.1.1.17 {ECO:0000250|UniProtKB:P11926};
DE Flags: Precursor;
GN Name=ODC {ECO:0000303|PubMed:21232776};
OS Nicotiana glauca (Glaucous tobacco) (Tree 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=4090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP PATHWAY.
RC STRAIN=cv. Melbourne 1; TISSUE=Leaf;
RX PubMed=21232776; DOI=10.1016/j.phytochem.2010.12.012;
RA DeBoer K.D., Dalton H.L., Edward F.J., Hamill J.D.;
RT "RNAi-mediated down-regulation of ornithine decarboxylase (ODC) leads to
RT reduced nicotine and increased anatabine levels in transgenic Nicotiana
RT tabacum L.";
RL Phytochemistry 72:344-355(2011).
RN [2]
RP INDUCTION BY WOUNDING.
RX PubMed=32688942; DOI=10.1071/fp03242;
RA Sinclair S.J., Johnson R., Hamill J.D.;
RT "Analysis of wound-induced gene expression in Nicotiana species with
RT contrasting alkaloid profiles.";
RL Funct. Plant Biol. 31:721-729(2004).
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:21232776). Catalyzes the first and
CC rate-limiting step of polyamine biosynthesis that converts ornithine
CC into putrescine, which is the precursor for the polyamines, spermidine
CC and spermine (By similarity). Polyamines are essential for cell
CC proliferation and are implicated in cellular processes, ranging from
CC DNA replication to apoptosis (By similarity).
CC {ECO:0000250|UniProtKB:P11926, ECO:0000269|PubMed:21232776}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-ornithine = CO2 + putrescine; Xref=Rhea:RHEA:22964,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:46911,
CC ChEBI:CHEBI:326268; EC=4.1.1.17;
CC Evidence={ECO:0000250|UniProtKB:P11926};
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:21232776}.
CC -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC L-ornithine pathway; putrescine from L-ornithine: step 1/1.
CC {ECO:0000250|UniProtKB:O22616}.
CC -!- SUBUNIT: Homodimer. Only the dimer is catalytically active, as the
CC active sites are constructed of residues from both monomers.
CC {ECO:0000250|UniProtKB:P11926}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- INDUCTION: Induced by wounding. {ECO:0000269|PubMed:32688942}.
CC -!- DISRUPTION PHENOTYPE: Reduced nicotine but increased anatabine
CC contents; these phenotypes are enhanced upon treatment with jasmonic
CC acid (MeJA) and wounding (e.g. removal of apices).
CC {ECO:0000269|PubMed:21232776}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC {ECO:0000305}.
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DR EMBL; FR691072; CBX19979.1; -; Genomic_DNA.
DR UniPathway; UPA00107; -.
DR UniPathway; UPA00535; UER00288.
DR GO; GO:0004586; F:ornithine decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0042179; P:nicotine biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:InterPro.
DR GO; GO:0009753; P:response to jasmonic acid; IMP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IMP:UniProtKB.
DR Gene3D; 2.40.37.10; -; 1.
DR Gene3D; 3.20.20.10; -; 1.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR022643; De-COase2_C.
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; IPR002433; Orn_de-COase.
DR InterPro; IPR029066; PLP-binding_barrel.
DR PANTHER; PTHR11482; PTHR11482; 1.
DR Pfam; PF02784; Orn_Arg_deC_N; 1.
DR Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR PRINTS; PR01179; ODADCRBXLASE.
DR PRINTS; PR01182; ORNDCRBXLASE.
DR SUPFAM; SSF50621; SSF50621; 1.
DR SUPFAM; SSF51419; SSF51419; 1.
DR PROSITE; PS00878; ODR_DC_2_1; 1.
DR PROSITE; PS00879; ODR_DC_2_2; 1.
PE 2: Evidence at transcript level;
KW Alkaloid metabolism; Chloroplast; Lyase; Plastid; Pyridoxal phosphate;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..433
FT /note="Ornithine decarboxylase, chloroplastic"
FT /id="PRO_0000455777"
FT ACT_SITE 378
FT /note="Proton donor; shared with dimeric partner"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 228
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 266
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 299..302
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 342..343
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07805"
FT BINDING 379
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P07805"
FT BINDING 407
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT SITE 225
FT /note="Stacks against the aromatic ring of pyridoxal
FT phosphate and stabilizes reaction intermediates"
FT /evidence="ECO:0000250|UniProtKB:P00860"
FT MOD_RES 96
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P11926"
SQ SEQUENCE 433 AA; 46574 MW; 221B53BB8554A340 CRC64;
MAGQTIIVSG LNPAAILQST IGGGASPTAA AAAENGTRKV IPLSRDALQD FMLSIITQKL
QDEKQPFYVL DLGEVVSLMD QWKSALPNIR PFYAVKCNPE PSFLSILSAM GSNFDCASRA
EIEYVLALGI SPDRIVFANP CKPESDIIFA AKVGVNLTTY DSEDEVYKIR KHHPKSELLL
RIKPMFDGNA RCPMGPKYGA LPEEVEPLLR AAQAARLTVS GVSFHIGSGD ADSNAYLGAI
AAAKEVFETA AKLGMSKMTV LDVGGGFTSG HQFTAAAVAV KSALKQRFDD EPELTIIAEP
GRFFAETAFT LATTIIGKRV RGELREYWIN DGLYGSMNCV LYDHATVNAT PLAVQSNRSN
VTCGGSKTFP TTVFGPTCDA LDTVLRDYQL PELQVNDWLV FPNMGAYTKA AGSNFNGFNT
SAIVTHLAYA YPS
