DCOR_SOLLC
ID DCOR_SOLLC Reviewed; 431 AA.
AC O22616; O82420;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Ornithine decarboxylase;
DE Short=ODC;
DE EC=4.1.1.17;
DE AltName: Full=LeODC;
GN Name=ODC;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Pink ball; TISSUE=Root;
RA Kwak S.H., Lee S.H.;
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Rutgers; TISSUE=Ovary;
RX PubMed=9733552; DOI=10.1104/pp.118.1.323;
RA Alabadi D., Carbonell J.;
RT "Expression of ornithine decarboxylase is transiently increased by
RT pollination, 2,4-dichlorophenoxyacetic acid, and gibberellic acid in tomato
RT ovaries.";
RL Plant Physiol. 118:323-328(1998).
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 -!- TISSUE SPECIFICITY: High expression in roots, shoot tips and whole
CC flowers at anthesis. Lower expression in stems and the lowest in adult
CC leaves. {ECO:0000269|PubMed:9733552}.
CC -!- DEVELOPMENTAL STAGE: Transient induction at 8 days post-anthesis. ODC
CC activity seems to be related to active cell division.
CC {ECO:0000269|PubMed:9733552}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC {ECO:0000305}.
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DR EMBL; AF029349; AAB82301.2; -; mRNA.
DR EMBL; AF030292; AAC61845.1; -; mRNA.
DR RefSeq; NP_001234616.1; NM_001247687.1.
DR AlphaFoldDB; O22616; -.
DR SMR; O22616; -.
DR STRING; 4081.Solyc04g082030.1.1; -.
DR PaxDb; O22616; -.
DR PRIDE; O22616; -.
DR EnsemblPlants; Solyc04g082030.1.1; Solyc04g082030.1.1.1; Solyc04g082030.1.
DR GeneID; 544209; -.
DR Gramene; Solyc04g082030.1.1; Solyc04g082030.1.1.1; Solyc04g082030.1.
DR KEGG; sly:544209; -.
DR eggNOG; KOG0622; Eukaryota.
DR HOGENOM; CLU_026444_1_0_1; -.
DR InParanoid; O22616; -.
DR OMA; CPEQPWH; -.
DR OrthoDB; 725914at2759; -.
DR PhylomeDB; O22616; -.
DR BioCyc; MetaCyc:MON-14991; -.
DR UniPathway; UPA00535; UER00288.
DR Proteomes; UP000004994; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; Polyamine biosynthesis; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..431
FT /note="Ornithine decarboxylase"
FT /id="PRO_0000239255"
FT ACT_SITE 376
FT /note="Proton donor; shared with dimeric partner"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 226
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 264
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 297..300
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 340..341
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07805"
FT BINDING 377
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P07805"
FT BINDING 405
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT SITE 223
FT /note="Stacks against the aromatic ring of pyridoxal
FT phosphate and stabilizes reaction intermediates"
FT /evidence="ECO:0000250|UniProtKB:P00860"
FT MOD_RES 94
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P11926"
SQ SEQUENCE 431 AA; 46647 MW; B126D4FECEAE305D CRC64;
MAGQTVIVSG LNPAAILQST IGGAPVAAAA ENGHTRKVVP LSKDALQDFM VSIITQKLQD
DKQPFYVLDL GEVVSLMEQW NSALPNIRPF YAVKCNPEPS FLSMLSAMGS NFDCASRAEI
EYVLSHGISP DRIVFANPCK PESDIIFAEK IGVNLTTYDS EDEVYKIRKH HPKCELLLRI
KPMTDGNARC PMGPKYGALP EEIEPLLRTA QAARLTVSGV SFHIGSGDAD SNAYLGAIAA
AKQVFETAAQ LGMPKMTVLD IGGGFTSGHQ FTTAAPAVKS ALETHFHDFP ELTIIAEPGR
FFAETAFTLA TTIIGKRVRG ELKEYWINDG LYGSMNCVLY DHATVTATPL ACMSNRNNLN
CGGSKTFPST VFGPTCDALD TVLRDYQLPE LQVNDWLIFP NMGAYTKAAG SNFNGFNTSA
IVTHLAYAYP N
