ID   DCOR_DATST              Reviewed;         431 AA.
AC   P50134;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Ornithine decarboxylase;
DE            Short=ODC;
DE            EC=4.1.1.17;
OS   Datura stramonium (Jimsonweed) (Common thornapple).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Datureae; Datura.
OX   NCBI_TaxID=4076;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. D15/5; TISSUE=Root;
RX   PubMed=8660289; DOI=10.1042/bj3140241;
RA   Michael A.J., Furze J.M., Rhodes M.J.C., Burtin D.;
RT   "Molecular cloning and functional identification of a plant ornithine
RT   decarboxylase cDNA.";
RL   Biochem. J. 314:241-248(1996).
CC   -!- FUNCTION: Catalyzes the first and rate-limiting step of polyamine
CC       biosynthesis that converts ornithine into putrescine, which is the
CC       precursor for the polyamines, spermidine and spermine. Polyamines are
CC       essential for cell proliferation and are implicated in cellular
CC       processes, ranging from DNA replication to apoptosis.
CC       {ECO:0000250|UniProtKB:P11926}.
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   -!- ACTIVITY REGULATION: Inhibited by antizyme (AZ) in response to
CC       polyamine levels. AZ inhibits the assembly of the functional homodimer
CC       by binding to ODC monomers and targeting them for ubiquitin-independent
CC       proteolytic destruction by the 26S proteasome.
CC       {ECO:0000250|UniProtKB:P11926}.
CC   -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC       L-ornithine pathway; putrescine from L-ornithine: step 1/1.
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   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X87847; CAA61121.1; -; mRNA.
DR   PIR; S64704; S64704.
DR   AlphaFoldDB; P50134; -.
DR   SMR; P50134; -.
DR   BioCyc; MetaCyc:MON-14990; -.
DR   UniPathway; UPA00535; UER00288.
DR   GO; GO:0004586; F:ornithine decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0033387; P:putrescine biosynthetic process from ornithine; IEA:UniProtKB-UniPathway.
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   Decarboxylase; Lyase; Polyamine biosynthesis; Pyridoxal phosphate.
FT   CHAIN           1..431
FT                   /note="Ornithine decarboxylase"
FT                   /id="PRO_0000149904"
FT   ACT_SITE        376
FT                   /note="Proton donor; shared with dimeric partner"
FT                   /evidence="ECO:0000250|UniProtKB:P11926"
FT   BINDING         226
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P11926"
FT   BINDING         264
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P11926"
FT   BINDING         297..300
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P11926"
FT   BINDING         340..341
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P07805"
FT   BINDING         377
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P07805"
FT   BINDING         405
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P11926"
FT   SITE            223
FT                   /note="Stacks against the aromatic ring of pyridoxal
FT                   phosphate and stabilizes reaction intermediates"
FT                   /evidence="ECO:0000250|UniProtKB:P00860"
FT   MOD_RES         94
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P11926"
SQ   SEQUENCE   431 AA;  46659 MW;  8168064D8CC1C9F8 CRC64;
     MAGQTVIVSG LNPAAILQST IGGATPAPAA ENDHTRKVVP LSRDALQDFM VSIITQKLQD
     EKQPFYVLDL GEVVSLMDQW NAGLPNIRPF YAVKCNPEPS FLSMLSAMGS NFDCASRAEI
     EYVLSLGISP DRIVFANPCK PESDIIFAAK VGVNLTTFDS EDEVYKIRKH HPKCELLLRI
     KPMDDGNARC PMGPKYGALP EEVEPLLRTA QAARLTVSGV SFHIGSGDAD SKAYLGAIAA
     AKGVFETAAR FGMSKMTVLD IGGGFTSGHQ FTTASAAVRS ALEQHFHDEQ ELTIIAEPGR
     FFAETAFTLA TTIIGKRVRG ELREYWINDG LYGSMNCVLY DHATVNATPL ACMSNRSNLN
     CGGSKTFPST VFGPTCDALD TVLRDYQLPE LQVNDWLIFP NMGAYTKAAG SNFNGFNTSA
     IVTHLAYAYP S