DCOR_CAPAN
ID DCOR_CAPAN Reviewed; 435 AA.
AC Q8S3N2; Q84UH2;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Ornithine decarboxylase;
DE Short=ODC;
DE EC=4.1.1.17;
DE AltName: Full=CaODC1;
DE AltName: Full=CapODC;
GN Name=ODC; Synonyms=CUKM10;
OS Capsicum annuum (Capsicum pepper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX NCBI_TaxID=4072;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=cv. MC11; TISSUE=Fruit;
RX PubMed=14972797; DOI=10.1080/1025814021000036151;
RA Zainal Z., Sajari R., Ismail I.;
RT "Molecular cloning and sequence analysis of a cDNA encoding ornithine
RT decarboxylase cDNA from chilli (Capsicum annuum).";
RL J. Biochem. Mol. Biol. Biophys. 6:415-419(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RA Yoo T.H., Park C.-J., Lee G.-J., Shin R., Kim K.-J., Yun J.-H., Paek K.-H.;
RT "A hot pepper cDNA encoding ornithine decarboxylase is induced during the
RT resistance response to tobacco mosaic virus.";
RL Submitted (FEB-2002) 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 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 -!- INDUCTION: By virus infection. Up-regulated during the later stages of
CC ripening. {ECO:0000269|PubMed:14972797, ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC {ECO:0000305}.
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DR EMBL; AF480882; AAL87201.1; -; mRNA.
DR EMBL; AY078081; AAL83709.1; -; mRNA.
DR RefSeq; NP_001311857.1; NM_001324928.1.
DR AlphaFoldDB; Q8S3N2; -.
DR SMR; Q8S3N2; -.
DR GeneID; 107866830; -.
DR KEGG; cann:107866830; -.
DR BioCyc; MetaCyc:MON-14989; -.
DR UniPathway; UPA00535; UER00288.
DR Proteomes; UP000189700; Genome assembly.
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..435
FT /note="Ornithine decarboxylase"
FT /id="PRO_0000239254"
FT ACT_SITE 380
FT /note="Proton donor; shared with dimeric partner"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 230
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 268
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 301..304
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 344..345
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07805"
FT BINDING 381
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P07805"
FT BINDING 409
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT SITE 227
FT /note="Stacks against the aromatic ring of pyridoxal
FT phosphate and stabilizes reaction intermediates"
FT /evidence="ECO:0000250|UniProtKB:P00860"
FT MOD_RES 98
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT CONFLICT 65
FT /note="E -> K (in Ref. 2; AAL83709)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="R -> H (in Ref. 2; AAL83709)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="V -> D (in Ref. 2; AAL83709)"
FT /evidence="ECO:0000305"
FT CONFLICT 391..392
FT /note="HV -> QL (in Ref. 2; AAL83709)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="V -> L (in Ref. 2; AAL83709)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 435 AA; 46906 MW; CC38830BFD7B1B76 CRC64;
MAGQTVIVSG LNPAAILQST IGGAPPSTAA AAAENGDTTR KVVPLSKDAL QDFMVSIITQ
KLQGEKKPFY VLDLGEVVSL MDQWNVALPN VRPFYAVKCN PEPSFLSMLA AMGSNFVCAS
RAEIEYVLSL GISPERIVFA NPCKPESDII FAEKVGVNLT TYDSEDEVYK IKKHHPKCEL
LLRIKPMNDG NARCPMGPKY GALPEEIEPL LRIAQASRLT VSGVSFHIGS GDADSNAYLG
AIAAAKQVFE TAAKFGMSKM NVLDIGGGFT SGHQFTTAAT AVKSALQQHF SNEPELTIIA
EPGRFFAETA FTLATTIIGK RVRGDLREYW INDGLYGSMN CVLYDHATVT ATPLACMSNR
VNLNCSGSKM FPSTIFGPTC DALDTVLRDY HVPELQVNDW VIFPNMGAYT KAAGSNFNGF
NTSAIVTHLA YAYPS
