DCOR_PANRE
ID DCOR_PANRE Reviewed; 435 AA.
AC P49725;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Ornithine decarboxylase;
DE Short=ODC;
DE EC=4.1.1.17;
GN Name=ODC;
OS Panagrellus redivivus (Microworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Panagrolaimoidea; Panagrolaimidae;
OC Panagrellus.
OX NCBI_TaxID=6233;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7772052; DOI=10.1042/bj3080635;
RA von Besser H., Niemann G., Domdey B., Walter R.D.;
RT "Molecular cloning and characterization of ornithine decarboxylase cDNA of
RT the nematode Panagrellus redivivus.";
RL Biochem. J. 308:635-640(1995).
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 -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC {ECO:0000305}.
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DR EMBL; X82199; CAA57683.1; -; mRNA.
DR EMBL; X95719; CAA65024.1; -; Genomic_DNA.
DR PIR; S55347; S52784.
DR AlphaFoldDB; P49725; -.
DR SMR; P49725; -.
DR SABIO-RK; P49725; -.
DR UniPathway; UPA00535; UER00288.
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; 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_0000149902"
FT ACT_SITE 368
FT /note="Proton donor; shared with dimeric partner"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 207
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 244
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 283..286
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 339..340
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07805"
FT BINDING 369
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P07805"
FT BINDING 397
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT SITE 204
FT /note="Stacks against the aromatic ring of pyridoxal
FT phosphate and stabilizes reaction intermediates"
FT /evidence="ECO:0000250|UniProtKB:P00860"
FT MOD_RES 76
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P11926"
SQ SEQUENCE 435 AA; 47111 MW; BBB093C1EF7FEFA4 CRC64;
MTLTGCVDYY EIIAGTKVAV CRNAIDNKTV ATAIAATRTV NGNDDPFVVM NVSTIMAKVI
QWQRTMPRVA PCYAVKCNDD KVLLRTLADL GMGFDCASKA EIEKVIGLVG PEKIVYANPC
KTRGFIAHAE AAGVKRMTFD SVEELTKIKQ NHADPSLILR ISVSDPTAQC QLGIKFGCDP
ETVAPKLLRK AADMGMNVIG ISFHVGSGCN EPATFRTALE YARGLFDLGI SLGLSMTLLD
IGGGFPGVDT AHISLDACAA VINPALEELF PLDSCPDVEV IAEPGRYFAC AAVSVTTNVI
ASVKVPASRI TEKADDVNRD GYMYYMNDGV YGSFNCKLFD HYQPRGMPLA EHDADEPRFP
VCVWGPTCDG LDQVEESSVM PRLYEGDWLY YPDMGAYTSV AASTFNGFDK PKTYYFIDEA
TLGSIVRKAD SAPRG
