ID   DCOR_PARBR              Reviewed;          79 AA.
AC   Q92445;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Ornithine decarboxylase;
DE            Short=ODC;
DE            EC=4.1.1.17;
DE   Flags: Fragment;
GN   Name=ODC;
OS   Paracoccidioides brasiliensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=121759;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 32071 / IVIC Pb73 / C81;
RX   PubMed=8661922; DOI=10.1007/s002030050332;
RA   San-Blas G., Sorais F., San-Blas F., Ruiz-Herrera J.;
RT   "Ornithine decarboxylase in Paracoccidioides brasiliensis.";
RL   Arch. Microbiol. 165:311-316(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:P08432}.
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:P08432};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P08432};
CC   -!- ACTIVITY REGULATION: Inhibited by antizyme (AZ) OAZ1 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:P08432}.
CC   -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC       L-ornithine pathway; putrescine from L-ornithine: step 1/1.
CC   -!- SUBUNIT: Homodimer (By similarity). Only the dimer is catalytically
CC       active, as the active sites are constructed of residues from both
CC       monomers (By similarity). {ECO:0000250|UniProtKB:P08432,
CC       ECO:0000250|UniProtKB:P11926}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08432}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       {ECO:0000305}.
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DR   EMBL; X97265; CAA65920.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q92445; -.
DR   SMR; Q92445; -.
DR   VEuPathDB; FungiDB:PABG_00600; -.
DR   VEuPathDB; FungiDB:PADG_03032; -.
DR   UniPathway; UPA00535; UER00288.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 3.20.20.10; -; 1.
DR   InterPro; IPR022657; De-COase2_CS.
DR   InterPro; IPR022644; De-COase2_N.
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   SUPFAM; SSF51419; SSF51419; 1.
DR   PROSITE; PS00879; ODR_DC_2_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Decarboxylase; Lyase; Polyamine biosynthesis;
KW   Pyridoxal phosphate.
FT   CHAIN           <1..>79
FT                   /note="Ornithine decarboxylase"
FT                   /id="PRO_0000149907"
FT   BINDING         8
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P11926"
FT   BINDING         45
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P11926"
FT   BINDING         75..78
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P11926"
FT   SITE            5
FT                   /note="Stacks against the aromatic ring of pyridoxal
FT                   phosphate and stabilizes reaction intermediates"
FT                   /evidence="ECO:0000250|UniProtKB:P00860"
FT   NON_TER         1
FT   NON_TER         79
SQ   SEQUENCE   79 AA;  8579 MW;  3F81351DC5C84F9B CRC64;
     GVSFHVGSGA EDPKSFVKAV EDSRFVFDQA AEVGFDLKVL DVGGGFSEDT FERFAATLSD
     ALDEYFPPHI RIIAEPGRI