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Ornithine decarboxylase (ODC) (EC 4.1.1.17)

 DCOR_CAEEL              Reviewed;         422 AA.
P41931; Q94278;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
11-JAN-2001, sequence version 2.
18-JUL-2018, entry version 127.
RecName: Full=Ornithine decarboxylase;
Short=ODC;
EC=4.1.1.17 {ECO:0000269|PubMed:7498733, ECO:0000305|PubMed:19762559};
Name=odc-1 {ECO:0000312|WormBase:K11C4.4};
ORFNames=K11C4.4 {ECO:0000312|WormBase:K11C4.4};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
PATHWAY, AND DISRUPTION PHENOTYPE.
STRAIN=Bristol N2;
PubMed=7498733;
Macrae M., Plasterk R.H., Coffino P.;
"The ornithine decarboxylase gene of Caenorhabditis elegans: cloning,
mapping and mutagenesis.";
Genetics 140:517-525(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3]
FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
PubMed=19762559; DOI=10.1096/fj.09-135889;
Heinick A., Urban K., Roth S., Spies D., Nunes F., Phanstiel O. IV,
Liebau E., Lueersen K.;
"Caenorhabditis elegans P5B-type ATPase CATP-5 operates in polyamine
transport and is crucial for norspermidine-mediated suppression of RNA
interference.";
FASEB J. 24:206-217(2010).
-!- FUNCTION: Catalyzes the first and rate-limiting step of polyamine
biosynthesis that converts ornithine into putrescine, which is the
precursor for the polyamines, spermidine and spermine
(PubMed:7498733, PubMed:19762559). Polyamines are essential for
cell proliferation and are implicated in cellular processes,
ranging from DNA replication to apoptosis (PubMed:19762559).
{ECO:0000269|PubMed:19762559, ECO:0000269|PubMed:7498733}.
-!- CATALYTIC ACTIVITY: L-ornithine = putrescine + CO(2).
{ECO:0000269|PubMed:7498733, ECO:0000305|PubMed:19762559}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000250|UniProtKB:P11926};
-!- ENZYME REGULATION: Inhibited by antizyme (AZ) in response to
polyamine levels. AZ inhibits the assembly of the functional
homodimer by binding to ODC monomers and targeting them for
ubiquitin-independent proteolytic destruction by the 26S
proteasome. {ECO:0000250|UniProtKB:P11926}.
-!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis
via L-ornithine pathway; putrescine from L-ornithine: step 1/1.
{ECO:0000269|PubMed:7498733}.
-!- SUBUNIT: Homodimer. Only the dimer is catalytically active, as the
active sites are constructed of residues from both monomers.
{ECO:0000250|UniProtKB:P11926}.
-!- DISRUPTION PHENOTYPE: Deletion mutant pc13 has a reduced brood
size and reduced enzymatic activity (PubMed:7498733). Smaller body
size as compared to wild-type. Reduced putrescine and spermidine
levels (PubMed:19762559). Double knockout with the polyamine
transporter catp-5 results in a reduced brood size, delayed
postembryonic development, and a more marked reduction in
putrescine and spermidine levels as compared to the single mutants
(PubMed:19762559). {ECO:0000269|PubMed:19762559,
ECO:0000269|PubMed:7498733}.
-!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II
family. {ECO:0000305}.
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EMBL; U03059; AAA88795.1; -; Genomic_DNA.
EMBL; FO081626; CCD72902.1; -; Genomic_DNA.
PIR; T29143; T29143.
RefSeq; NP_504752.1; NM_072351.6.
UniGene; Cel.17530; -.
ProteinModelPortal; P41931; -.
SMR; P41931; -.
STRING; 6239.K11C4.4.1; -.
EPD; P41931; -.
PaxDb; P41931; -.
PeptideAtlas; P41931; -.
PRIDE; P41931; -.
EnsemblMetazoa; K11C4.4; K11C4.4; WBGene00003844.
GeneID; 179079; -.
KEGG; cel:CELE_K11C4.4; -.
UCSC; K11C4.4.1; c. elegans.
CTD; 179079; -.
WormBase; K11C4.4; CE12114; WBGene00003844; odc-1.
eggNOG; KOG0622; Eukaryota.
eggNOG; COG0019; LUCA.
GeneTree; ENSGT00390000011560; -.
HOGENOM; HOG000274133; -.
InParanoid; P41931; -.
KO; K01581; -.
OMA; VVGYICE; -.
OrthoDB; EOG091G0AJV; -.
PhylomeDB; P41931; -.
UniPathway; UPA00535; UER00288.
PRO; PR:P41931; -.
Proteomes; UP000001940; Chromosome V.
Bgee; WBGene00003844; -.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0004586; F:ornithine decarboxylase activity; IBA:GO_Central.
GO; GO:0033387; P:putrescine biosynthetic process from ornithine; IBA:GO_Central.
Gene3D; 2.40.37.10; -; 2.
Gene3D; 3.20.20.10; -; 1.
InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
InterPro; IPR022643; De-COase2_C.
InterPro; IPR022644; De-COase2_N.
InterPro; IPR022653; De-COase2_pyr-phos_BS.
InterPro; IPR000183; Orn/DAP/Arg_de-COase.
InterPro; IPR002433; Orn_de-COase.
InterPro; IPR029066; PLP-binding_barrel.
PANTHER; PTHR11482; PTHR11482; 1.
Pfam; PF02784; Orn_Arg_deC_N; 1.
Pfam; PF00278; Orn_DAP_Arg_deC; 1.
PRINTS; PR01179; ODADCRBXLASE.
PRINTS; PR01182; ORNDCRBXLASE.
SUPFAM; SSF50621; SSF50621; 1.
SUPFAM; SSF51419; SSF51419; 1.
PROSITE; PS00878; ODR_DC_2_1; 1.
PROSITE; PS00879; ODR_DC_2_2; 1.
1: Evidence at protein level;
Complete proteome; Decarboxylase; Lyase; Polyamine biosynthesis;
Pyridoxal phosphate; Reference proteome.
CHAIN 1 422 Ornithine decarboxylase.
/FTId=PRO_0000149898.
REGION 275 278 Pyridoxal phosphate binding.
{ECO:0000250|UniProtKB:P11926}.
REGION 331 332 Substrate binding.
{ECO:0000250|UniProtKB:P07805}.
ACT_SITE 359 359 Proton donor; shared with dimeric
partner. {ECO:0000250|UniProtKB:P11926}.
BINDING 203 203 Pyridoxal phosphate.
{ECO:0000250|UniProtKB:P11926}.
BINDING 240 240 Pyridoxal phosphate; via amino nitrogen.
{ECO:0000250|UniProtKB:P11926}.
BINDING 360 360 Substrate; shared with dimeric partner.
{ECO:0000250|UniProtKB:P07805}.
BINDING 388 388 Pyridoxal phosphate.
{ECO:0000250|UniProtKB:P11926}.
SITE 200 200 Stacks against the aromatic ring of
pyridoxal phosphate and stabilizes
reaction intermediates.
{ECO:0000250|UniProtKB:P00860}.
MOD_RES 71 71 N6-(pyridoxal phosphate)lysine.
{ECO:0000250|UniProtKB:P11926}.
CONFLICT 273 274 IA -> YR (in Ref. 1; AAA88795).
{ECO:0000305}.
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


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