DCOR_CRIGR
ID DCOR_CRIGR Reviewed; 455 AA.
AC P14019;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 3.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Ornithine decarboxylase;
DE Short=ODC;
DE EC=4.1.1.17;
GN Name=ODC1; Synonyms=ODC;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2602162; DOI=10.1093/nar/17.24.10497;
RA Grens A., Steglich C., Pilz R., Scheffler I.E.;
RT "Nucleotide sequence of the Chinese hamster ornithine decarboxylase gene.";
RL Nucleic Acids Res. 17:10497-10497(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 163-455.
RX PubMed=2887574; DOI=10.1016/s0021-9258(18)45287-8;
RA Srinivasan P.R., Tonin P.N., Wensing E.J., Lewis W.H.;
RT "The gene for ornithine decarboxylase is co-amplified in hydroxyurea-
RT resistant hamster cells.";
RL J. Biol. Chem. 262:12871-12878(1987).
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; X16910; CAA34784.1; -; mRNA.
DR EMBL; J02813; AAA36963.1; -; mRNA.
DR PIR; S09574; DCHYOC.
DR AlphaFoldDB; P14019; -.
DR SMR; P14019; -.
DR STRING; 10029.XP_007633536.1; -.
DR eggNOG; KOG0622; Eukaryota.
DR UniPathway; UPA00535; UER00288.
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; 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; S-nitrosylation.
FT CHAIN 1..455
FT /note="Ornithine decarboxylase"
FT /id="PRO_0000149890"
FT ACT_SITE 354
FT /note="Proton donor; shared with dimeric partner"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 197
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 234
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 271..274
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 325..326
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07805"
FT BINDING 355
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P07805"
FT BINDING 383
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT SITE 194
FT /note="Stacks against the aromatic ring of pyridoxal
FT phosphate and stabilizes reaction intermediates"
FT /evidence="ECO:0000250|UniProtKB:P00860"
FT MOD_RES 67
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT MOD_RES 297
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:P00860"
FT MOD_RES 354
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT CONFLICT 452
FT /note="S -> R (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 455 AA; 50454 MW; 14162985F188C89F CRC64;
MNSFNKDEFD CHILDEGFTA KDILDQKINE VSSDDKDAFY VADLGDVLKK HLRWLKALPV
TPFYAVKCND SRALVNTLAA ITVDCASKTE IQLVQGLGVP PERVIYANPC KQVSQIKYAA
SNGVQMMTFD SEIELMKVAR AHPKVTKLVL RIATDDSKAV CRLSVKFGAT LRTSRLLLER
AKELNIDVIG VSFHVGSGCT DPETFVQALS DARCVFDMGT EVGFSMYLLD IGGGFPGSED
TKLKFEEITS VINPALDKYF PPDSGVRVIA EPGRYYVASA FTLAVNIIAK KIVSKGSDDE
DESSEQTFMY YVNDGVYGSF NCILYDHAHV KPLLPKRPKP DEKYYSSSIW GPTCDGLDRI
VERCNLPEMH VGDWMLFENM GAYTVAAAST FNGFQRPSIY YVMSRPMWQL MKQIQNHGFP
PEVEEQDVGT LPISCAQESG MDRHPAACAS ASINV
