DCOR_CHICK
ID DCOR_CHICK Reviewed; 450 AA.
AC P27118;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Ornithine decarboxylase;
DE Short=ODC;
DE EC=4.1.1.17;
DE Flags: Fragment;
GN Name=ODC1; Synonyms=ODC;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn;
RX PubMed=1416246; DOI=10.1111/j.1365-2052.1992.tb02158.x;
RA Johnson R., Bulfield G.;
RT "Molecular cloning and sequence analysis of a chicken ornithine
RT decarboxylase cDNA.";
RL Anim. Genet. 23:403-409(1992).
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) in response to
CC polyamine levels. AZs inhibit 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}.
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DR EMBL; X64710; CAA45965.1; -; mRNA.
DR PIR; A48386; DCCHO.
DR RefSeq; NP_001161238.1; NM_001167766.1.
DR AlphaFoldDB; P27118; -.
DR SMR; P27118; -.
DR STRING; 9031.ENSGALP00000026476; -.
DR PaxDb; P27118; -.
DR GeneID; 421937; -.
DR KEGG; gga:421937; -.
DR CTD; 101892980; -.
DR VEuPathDB; HostDB:geneid_421937; -.
DR eggNOG; KOG0622; Eukaryota.
DR InParanoid; P27118; -.
DR OrthoDB; 725914at2759; -.
DR PhylomeDB; P27118; -.
DR UniPathway; UPA00535; UER00288.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0004586; F:ornithine decarboxylase activity; IBA:GO_Central.
DR GO; GO:0033387; P:putrescine biosynthetic process from ornithine; IBA:GO_Central.
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.
FT CHAIN <1..450
FT /note="Ornithine decarboxylase"
FT /id="PRO_0000149895"
FT ACT_SITE 350
FT /note="Proton donor; shared with dimeric partner"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 190
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 227
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 264..267
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 321..322
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07805"
FT BINDING 351
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P07805"
FT BINDING 379
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT SITE 187
FT /note="Stacks against the aromatic ring of pyridoxal
FT phosphate and stabilizes reaction intermediates"
FT /evidence="ECO:0000250|UniProtKB:P00860"
FT MOD_RES 59
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT MOD_RES 293
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 450 AA; 49735 MW; 5EAC75DF3D17AD2C CRC64;
FTFLDEGFTA KDILDQKINE VSSSDDKDAF YVADLGDIVK KHMRWHKALP RVTPFYAVKC
NDSEAVVKTL AVLGAGFDCA SKTEIQLVQS IGVPPERIIY ANPCKQLSQI KHAANSGVRM
MTFDSEVELM KIARPHPKAK LLLRITTDDS KAVCRLSVKF GATLKTSRLL LERAKELDLA
IVGVSFHVGS GCTDPETFVQ AISDARCVFD MGAELGFNMY LLDIGGGFPG SEDVKLKFEE
ITSVINPALD KYFPLDSEVT IIAEPGRYYV ASAFTLAVNI IAKKIVSKEQ TGSDDEDDVN
DKTLMYYVND GVYGSFNCIL YDHAHVKPVL QKRPKPDDGC YSCSIWGPTC DGLDRIVERC
NMPELQVGDW ILFENMGAYT VAAASTFNGF QRPTIHYVMS RPAWQLMQQI KEQEFLAEVE
EQDVASLPLS CACESGIEYP ATCASASINV
