DCOR_CAEEL
ID DCOR_CAEEL Reviewed; 422 AA.
AC P41931; Q94278;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Ornithine decarboxylase;
DE Short=ODC;
DE EC=4.1.1.17 {ECO:0000269|PubMed:7498733, ECO:0000305|PubMed:19762559};
GN Name=odc-1 {ECO:0000312|WormBase:K11C4.4};
GN ORFNames=K11C4.4 {ECO:0000312|WormBase:K11C4.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2;
RX PubMed=7498733; DOI=10.1093/genetics/140.2.517;
RA Macrae M., Plasterk R.H., Coffino P.;
RT "The ornithine decarboxylase gene of Caenorhabditis elegans: cloning,
RT mapping and mutagenesis.";
RL Genetics 140:517-525(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19762559; DOI=10.1096/fj.09-135889;
RA Heinick A., Urban K., Roth S., Spies D., Nunes F., Phanstiel O. IV,
RA Liebau E., Lueersen K.;
RT "Caenorhabditis elegans P5B-type ATPase CATP-5 operates in polyamine
RT transport and is crucial for norspermidine-mediated suppression of RNA
RT interference.";
RL FASEB J. 24:206-217(2010).
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 (PubMed:7498733,
CC PubMed:19762559). Polyamines are essential for cell proliferation and
CC are implicated in cellular processes, ranging from DNA replication to
CC apoptosis (PubMed:19762559). {ECO:0000269|PubMed:19762559,
CC ECO:0000269|PubMed:7498733}.
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:0000269|PubMed:7498733, ECO:0000305|PubMed:19762559};
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 {ECO:0000269|PubMed:7498733}.
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 -!- DISRUPTION PHENOTYPE: Deletion mutant pc13 has a reduced brood size and
CC reduced enzymatic activity (PubMed:7498733). Smaller body size as
CC compared to wild-type. Reduced putrescine and spermidine levels
CC (PubMed:19762559). Double knockout with the polyamine transporter catp-
CC 5 results in a reduced brood size, delayed postembryonic development,
CC and a more marked reduction in putrescine and spermidine levels as
CC compared to the single mutants (PubMed:19762559).
CC {ECO:0000269|PubMed:19762559, ECO:0000269|PubMed:7498733}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC {ECO:0000305}.
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DR EMBL; U03059; AAA88795.1; -; Genomic_DNA.
DR EMBL; FO081626; CCD72902.1; -; Genomic_DNA.
DR PIR; T29143; T29143.
DR RefSeq; NP_504752.1; NM_072351.6.
DR AlphaFoldDB; P41931; -.
DR SMR; P41931; -.
DR BioGRID; 44124; 1.
DR STRING; 6239.K11C4.4.1; -.
DR EPD; P41931; -.
DR PaxDb; P41931; -.
DR PeptideAtlas; P41931; -.
DR EnsemblMetazoa; K11C4.4.1; K11C4.4.1; WBGene00003844.
DR GeneID; 179079; -.
DR KEGG; cel:CELE_K11C4.4; -.
DR UCSC; K11C4.4.1; c. elegans.
DR CTD; 179079; -.
DR WormBase; K11C4.4; CE12114; WBGene00003844; odc-1.
DR eggNOG; KOG0622; Eukaryota.
DR GeneTree; ENSGT00950000182995; -.
DR HOGENOM; CLU_026444_1_1_1; -.
DR InParanoid; P41931; -.
DR OMA; YCRSMAS; -.
DR OrthoDB; 725914at2759; -.
DR PhylomeDB; P41931; -.
DR Reactome; R-CEL-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-CEL-351143; Agmatine biosynthesis.
DR Reactome; R-CEL-351202; Metabolism of polyamines.
DR UniPathway; UPA00535; UER00288.
DR PRO; PR:P41931; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00003844; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004586; F:ornithine decarboxylase activity; IDA:WormBase.
DR GO; GO:0033387; P:putrescine biosynthetic process from ornithine; IDA:WormBase.
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 1: Evidence at protein level;
KW Decarboxylase; Lyase; Polyamine biosynthesis; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..422
FT /note="Ornithine decarboxylase"
FT /id="PRO_0000149898"
FT ACT_SITE 359
FT /note="Proton donor; shared with dimeric partner"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 203
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 240
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 275..278
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 360
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P07805"
FT BINDING 388
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT SITE 200
FT /note="Stacks against the aromatic ring of pyridoxal
FT phosphate and stabilizes reaction intermediates"
FT /evidence="ECO:0000250|UniProtKB:P00860"
FT MOD_RES 71
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT CONFLICT 273..274
FT /note="IA -> YR (in Ref. 1; AAA88795)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 46920 MW; DD2E9707EE846B1D CRC64;
MISQFEIIGD NKIGVLPKQV DQLQMCRDIA ASKDLQENDS SFMLVDLDKI IERFQLWKRE
LPMIEPFYAV KCNTDLVLIR ILASLGCGFD CASKDEIDIV MGTGVSAERI IYANPCKTRS
FIAHAMDRDV KMMTFDNPEE LLKIAKLHPN AEMILRIAVS DPTATCPLNL KFGADPIIAA
PQLLKTASEE GINVVGISFH VGSGCNDASA YRNALQHAKN LCEIGEGLGF KMDIIDMGGG
FPGAEHHNPF EKIAETIRDA LDEFFPDTNK RLIAEPGRFF AAGPFSLVAN IIHATEVPAS
KITKDPKDCA DHGYMYYIND GVYGSFNCIL FDHAHPIGSP LFDTDRNEKF MSTIWGPTCD
SLDLVEDKKL MPKMNVGEWL YYPDMGAYTL AAATTFNGFS KPVPMYVMSE EMWESIRDST
HV
