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Probable ornithine decarboxylase (ODC) (EC 4.1.1.17)

 DCOR_DICDI              Reviewed;         461 AA.
Q54UF3;
08-APR-2008, integrated into UniProtKB/Swiss-Prot.
24-MAY-2005, sequence version 1.
28-FEB-2018, entry version 88.
RecName: Full=Probable ornithine decarboxylase;
Short=ODC;
EC=4.1.1.17;
Name=odc; ORFNames=DDB_G0281109;
Dictyostelium discoideum (Slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyostelids; Dictyosteliales;
Dictyosteliaceae; Dictyostelium.
NCBI_TaxID=44689;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=15875012; DOI=10.1038/nature03481;
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
-!- 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. Polyamines
are essential for cell proliferation and are implicated in
cellular processes, ranging from DNA replication to apoptosis.
{ECO:0000250|UniProtKB:P11926}.
-!- CATALYTIC ACTIVITY: L-ornithine = putrescine + CO(2).
{ECO:0000250|UniProtKB:P11926}.
-!- 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.
-!- SUBUNIT: Homodimer. Only the dimer is catalytically active, as the
active sites are constructed of residues from both monomers.
{ECO:0000250|UniProtKB:P11926}.
-!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II
family. {ECO:0000305}.
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EMBL; AAFI02000040; EAL66851.1; -; Genomic_DNA.
RefSeq; XP_640823.1; XM_635731.1.
ProteinModelPortal; Q54UF3; -.
SMR; Q54UF3; -.
STRING; 44689.DDB0237755; -.
PaxDb; Q54UF3; -.
EnsemblProtists; EAL66851; EAL66851; DDB_G0281109.
GeneID; 8622878; -.
KEGG; ddi:DDB_G0281109; -.
dictyBase; DDB_G0281109; odc.
eggNOG; KOG0622; Eukaryota.
eggNOG; COG0019; LUCA.
InParanoid; Q54UF3; -.
KO; K01581; -.
OMA; NDKFSSG; -.
PhylomeDB; Q54UF3; -.
Reactome; R-DDI-351143; Agmatine biosynthesis.
Reactome; R-DDI-351202; Metabolism of polyamines.
UniPathway; UPA00535; UER00288.
PRO; PR:Q54UF3; -.
Proteomes; UP000002195; Chromosome 3.
Proteomes; UP000002195; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0004586; F:ornithine decarboxylase activity; ISS:dictyBase.
GO; GO:0009446; P:putrescine biosynthetic process; IMP:dictyBase.
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.
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.
3: Inferred from homology;
Complete proteome; Decarboxylase; Lyase; Polyamine biosynthesis;
Pyridoxal phosphate; Reference proteome.
CHAIN 1 461 Probable ornithine decarboxylase.
/FTId=PRO_0000328317.
REGION 317 320 Pyridoxal phosphate binding.
{ECO:0000250|UniProtKB:P11926}.
REGION 375 376 Substrate binding.
{ECO:0000250|UniProtKB:P07805}.
COMPBIAS 13 19 Poly-Asn.
ACT_SITE 402 402 Proton donor; shared with dimeric
partner. {ECO:0000250|UniProtKB:P11926}.
BINDING 247 247 Pyridoxal phosphate.
{ECO:0000250|UniProtKB:P11926}.
BINDING 284 284 Pyridoxal phosphate; via amino nitrogen.
{ECO:0000250|UniProtKB:P11926}.
BINDING 403 403 Substrate; shared with dimeric partner.
{ECO:0000250|UniProtKB:P07805}.
BINDING 431 431 Pyridoxal phosphate.
{ECO:0000250|UniProtKB:P11926}.
SITE 244 244 Stacks against the aromatic ring of
pyridoxal phosphate and stabilizes
reaction intermediates.
{ECO:0000250|UniProtKB:P00860}.
MOD_RES 116 116 N6-(pyridoxal phosphate)lysine.
{ECO:0000250|UniProtKB:P11926}.
SEQUENCE 461 AA; 51695 MW; 500BF0DC382CE846 CRC64;
MTGTKRNGEE VVNENNNNNV AEETNKKAKV DESSTETTES TSCSLLSRCE KLDIVRKELD
VKPWDQGKVT IQELITSLLD KTDRDAFFVA DVGVIIKQWQ KWVKNLPNVK PYYAVKCNPT
VGVLRVLDAL GTNYDCASRT EIESVLNLGV DPSRIIYANP CKQISALKFA RAHNVKLMTF
DNLSELEKIE KFFPEAELVL RIAPDDSKSV MRFGSKFGVH IDDCNDLLEM AKEMNLKVVG
VSFHVGSGCQ SGDSYADALI MVKSVFDMAK KLNMELTLVD VGGGFTGSDD EKFNAFTKVI
REKTAELFSP NVKIIAEPGR YFAAQSHTLA VTVISKRSIK QEDNRQHPRR TSNNMRQYNY
YLADGVYGSF NNTKFDYAKV EPLLLKPSTK QPTPCTLFGP TCDSIDVVLK DTQIPELKIG
DWLYFQDMGA YTIASSSSFN GFCPPPVYYY NSIPEEELKN L


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