DCOR1_XENLA
ID DCOR1_XENLA Reviewed; 460 AA.
AC P27120;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Ornithine decarboxylase 1;
DE Short=ODC 1;
DE Short=xODC1;
DE EC=4.1.1.17;
GN Name=odc1-a; Synonyms=odc, odc1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Oocyte;
RX PubMed=2088731; DOI=10.1242/dev.110.3.955;
RA Bassez T., Paris J., Omilli F., Dorel C., Osborne H.B.;
RT "Post-transcriptional regulation of ornithine decarboxylase in Xenopus
RT laevis oocytes.";
RL Development 110:955-962(1990).
RN [2]
RP DEVELOPMENTAL STAGE.
RX PubMed=1761057; DOI=10.1111/j.1432-1033.1991.tb16410.x;
RA Osborne H.B., Duval C., Ghoda L., Omilli F., Bassez T., Coffino P.;
RT "Expression and post-transcriptional regulation of ornithine decarboxylase
RT during early Xenopus development.";
RL Eur. J. Biochem. 202:575-581(1991).
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 antizymes (AZs) in response to
CC polyamine levels. AZs inhibit 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 -!- DEVELOPMENTAL STAGE: Levels increase in the embryos 1.5-2 hours after
CC fertilization and reach a maximum at 6 hours post-fertilization, then
CC decrease to a very low level in early gastrulating embryos (12 hours
CC post-fertilization). {ECO:0000269|PubMed:1761057}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC {ECO:0000305}.
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DR EMBL; X56316; CAA39760.1; -; mRNA.
DR PIR; A43563; A43563.
DR AlphaFoldDB; P27120; -.
DR SMR; P27120; -.
DR UniPathway; UPA00535; UER00288.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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; 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; Phosphoprotein; Polyamine biosynthesis;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..460
FT /note="Ornithine decarboxylase 1"
FT /id="PRO_0000149896"
FT ACT_SITE 361
FT /note="Proton donor; shared with dimeric partner"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 200
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 237
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 274..277
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 332..333
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07805"
FT BINDING 362
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P07805"
FT BINDING 390
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT SITE 197
FT /note="Stacks against the aromatic ring of pyridoxal
FT phosphate and stabilizes reaction intermediates"
FT /evidence="ECO:0000250|UniProtKB:P00860"
FT MOD_RES 69
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT MOD_RES 303
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 460 AA; 50830 MW; CC6F87FD165877EE CRC64;
MNSFSNDDFD FSFLEEGFSA RDIVEQKINE VSLSDDKDAF YVADFGDIVK KHVRWFKALP
RVTPFYAVKC NDGKAIVKTL SILGAGFDCA SKTEIQLVQS IGVSPERIIY ANPCKQVSQI
KYAASCGVEK MTFDSEVELM KVARNHPNAK LVLRIATDDS KAVCRLSVKF GATLKTSRLL
LERAKELNVD IIGVSFHVGS GCTDPQTYVQ AVSDARCVFD MGAELGFNMH LLDIGGGFPG
SEDVKLKFEE ITSVINPALD KYFPADSGVK IIAEPGRYYV ASSFTLAVNI IAKKVMVNEQ
SGSDDEEDAA NDKTLMYYVN DGVYGSFNCI LFDHAHVKPV LTKKPKPDEK FYSSSIWGPT
CDGLDRIVER FELPELQVGD WMLFENMGAY TVAAASTFNG FQRPTLYYVM SRPHWQLMHD
IKEHGILPEV PDLSALHVSC AQESGMELAP AVCTAASINV
