ID   DCOR_BOVIN              Reviewed;         461 AA.
AC   P27117; A6H7E8;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Ornithine decarboxylase;
DE            Short=ODC;
DE            EC=4.1.1.17;
GN   Name=ODC1; Synonyms=ODC;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Holstein; TISSUE=Liver;
RX   PubMed=7774801; DOI=10.1139/g95-041;
RA   Yao J., Zadworny D., Kuhnlein U., Hayes J.F.;
RT   "Molecular cloning of a bovine ornithine decarboxylase cDNA and its use in
RT   the detection of restriction fragment length polymorphisms in Holsteins.";
RL   Genome 38:325-331(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10520448; DOI=10.3109/10425179809008453;
RA   Yao J., Zadworny D., Aggrey S.E., Kuhnlein U., Hayes J.F.;
RT   "Bovine ornithine decarboxylase gene: cloning, structure and
RT   polymorphisms.";
RL   DNA Seq. 8:203-213(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal skin;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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 antizymes (AZs) OAZ1, OAZ2 and OAZ3
CC       in response to polyamine levels. AZs inhibit the assembly of the
CC       functional homodimer by binding to ODC monomers. Additionally, OAZ1
CC       targets ODC monomers for ubiquitin-independent proteolytic destruction
CC       by the 26S proteasome. {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:P00860}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       {ECO:0000305}.
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DR   EMBL; M92441; AAA92339.1; -; mRNA.
DR   EMBL; U36394; AAA79849.1; -; Genomic_DNA.
DR   EMBL; U18531; AAA86696.1; -; Genomic_DNA.
DR   EMBL; BC146218; AAI46219.1; -; mRNA.
DR   RefSeq; NP_776555.1; NM_174130.2.
DR   RefSeq; XP_005212975.1; XM_005212918.2.
DR   RefSeq; XP_005212976.1; XM_005212919.3.
DR   RefSeq; XP_010808467.1; XM_010810165.2.
DR   AlphaFoldDB; P27117; -.
DR   SMR; P27117; -.
DR   STRING; 9913.ENSBTAP00000005575; -.
DR   BindingDB; P27117; -.
DR   ChEMBL; CHEMBL3243912; -.
DR   PaxDb; P27117; -.
DR   PRIDE; P27117; -.
DR   Ensembl; ENSBTAT00000005575; ENSBTAP00000005575; ENSBTAG00000004256.
DR   GeneID; 281365; -.
DR   KEGG; bta:281365; -.
DR   CTD; 4953; -.
DR   VEuPathDB; HostDB:ENSBTAG00000004256; -.
DR   eggNOG; KOG0622; Eukaryota.
DR   GeneTree; ENSGT00950000182995; -.
DR   HOGENOM; CLU_026444_1_2_1; -.
DR   InParanoid; P27117; -.
DR   OMA; YCRSMAS; -.
DR   OrthoDB; 725914at2759; -.
DR   TreeFam; TF300760; -.
DR   Reactome; R-BTA-350562; Regulation of ornithine decarboxylase (ODC).
DR   Reactome; R-BTA-351202; Metabolism of polyamines.
DR   UniPathway; UPA00535; UER00288.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000004256; Expressed in spermatid and 108 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0004586; F:ornithine decarboxylase activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0033387; P:putrescine biosynthetic process from ornithine; ISS:UniProtKB.
DR   GO; GO:0042176; P:regulation of protein catabolic process; ISS: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   Decarboxylase; Lyase; Phosphoprotein; Polyamine biosynthesis;
KW   Pyridoxal phosphate; Reference proteome; S-nitrosylation.
FT   CHAIN           1..461
FT                   /note="Ornithine decarboxylase"
FT                   /id="PRO_0000149889"
FT   ACT_SITE        360
FT                   /note="Proton donor; shared with dimeric partner"
FT                   /evidence="ECO:0000250|UniProtKB:P11926"
FT   BINDING         200
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P11926"
FT   BINDING         237
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P11926"
FT   BINDING         274..277
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P11926"
FT   BINDING         331..332
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P07805"
FT   BINDING         361
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P07805"
FT   BINDING         389
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P11926"
FT   SITE            197
FT                   /note="Stacks against the aromatic ring of pyridoxal
FT                   phosphate and stabilizes reaction intermediates"
FT                   /evidence="ECO:0000250|UniProtKB:P00860"
FT   MOD_RES         69
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P11926"
FT   MOD_RES         303
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000250|UniProtKB:P00860"
FT   MOD_RES         360
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P11926"
SQ   SEQUENCE   461 AA;  51346 MW;  4E609B643E3B68FA CRC64;
     MNSFSNEEFD CHFLDEGFTA KDILDQKINE VSYSDDKDAF YVADLGDILK KHLRWLKALP
     RVTPFYAVKC NDSRTIVKTL AAIGTGFDCA SKTEIQLVQS LGVPPERIIY ANPCKQVSQI
     KYAANNGVQM MTFDSEVELM KVARAHPKAK LVLRIATDDS KAVCRLSVKF GATLKTSRLL
     LERAKELDID VIGVSFHVGS GCTDPETFVQ AISDARCVFD MGAEVGFNMY LLDIGGGFPG
     SEDVKLKFEE ITSVINPALD KYFPSDSGVR IIAEPGRYYV ASAFTLAVNI IAKKLVLKEQ
     TGSDDEEEST DRTFMYYVND GVYGSFNCIL YDHAHVKPLL QKRPKPDEKY YSSSIWGPTC
     DGLDRIVERC NLPEMHVGDW MLFENMGAYT VAAASTFNGF QRPTIYYVMS GPTWQLMQQI
     RTQDFPPGVE EPDVGPLPVS CAWESGMKRH SAACASTRIN V