DCOR_MUSPA
ID DCOR_MUSPA Reviewed; 461 AA.
AC P27119;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Ornithine decarboxylase;
DE Short=ODC;
DE EC=4.1.1.17;
GN Name=Odc1; Synonyms=Odc;
OS Mus pahari (Gairdner's shrew-mouse) (Coelomys pahari).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Coelomys.
OX NCBI_TaxID=10093;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1374399; DOI=10.1016/s0021-9258(19)50206-x;
RA Johannes G., Berger F.G.;
RT "Alterations in mRNA translation as a mechanism for the modification of
RT enzyme synthesis during evolution. The ornithine decarboxylase model.";
RL J. Biol. Chem. 267:10108-10115(1992).
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) OAZ1, OAZ2 and OAZ3
CC in response to polyamine levels. AZs inhibit the assembly of the
CC functional homodimer by binding to ODC monomers. Additionally, OAZ1
CC targets ODC monomers for ubiquitin-independent proteolytic destruction
CC by the 26S proteasome. {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:P00860}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC {ECO:0000305}.
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DR EMBL; M87223; AAA39847.1; -; mRNA.
DR PIR; I55356; I55356.
DR AlphaFoldDB; P27119; -.
DR SMR; P27119; -.
DR MGI; MGI:97402; Odc1.
DR UniPathway; UPA00535; UER00288.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0004586; F:ornithine decarboxylase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0033387; P:putrescine biosynthetic process from ornithine; ISS:UniProtKB.
DR GO; GO:0042176; P:regulation of protein catabolic process; ISS:UniProtKB.
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; S-nitrosylation.
FT CHAIN 1..461
FT /note="Ornithine decarboxylase"
FT /id="PRO_0000149893"
FT ACT_SITE 360
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 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 361
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P07805"
FT BINDING 389
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|UniProtKB:P00860"
FT MOD_RES 360
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P11926"
SQ SEQUENCE 461 AA; 51203 MW; 61ABBCBEEC7BFB92 CRC64;
MSSFTKEEFD CHILDEGFTA KDILDQKINE VSSSDDKDAF YVADLGDILK KHLRWLKALP
RVTPFYAVKC NDSRAIVSTL AATGTGFDCA SKTEIQLVQG LGVPPERIIY ANPCKQVSQI
KYAASSGVQM MTFDSEIELM KVARAHPKAK LVLRIATDDS KAVCRLSVKF GATLKTSRLL
LERAKELNID VIGVSFHVGS GCTDPETFVQ AVSDARCVFD MGTEVGFSMY LLDIGGGFPG
SEDTKLKFEE ITSVINPALD KYFPSDSGVR IIAEPGRYYV ASAFTLAVNI IAKKTVWKEQ
PGSDDEDESN EQTFMYYVND GVYGSFNCIL YDHAHVKALL QKRPKPDEKY YSSSIWGPTC
DGLDRIVERC NLPEMHVGDW MLFENMGAYT VAAASTFNGF QRPNIYYVMS RPMWQLMKRI
QSHGFPPEVE EQDDGTLPMS CAQESGMDHH SAACASARIN V
