DCOR_SCHPO
ID DCOR_SCHPO Reviewed; 432 AA.
AC Q9UQW9; P78829;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Ornithine decarboxylase;
DE Short=ODC;
DE EC=4.1.1.17;
GN Name=spe1; ORFNames=SPAC144.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Franceschetti M., Illingworth C., Mayer M.J., Michael A.J.;
RT "Isolation and characterisation of a cDNA for ornithine decarboxylase from
RT Schizosaccharomyces pombe.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 70-432.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
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:P08432}.
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:P08432};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P08432};
CC -!- ACTIVITY REGULATION: Inhibited by antizyme (AZ) OAZ1 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:P08432}.
CC -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC L-ornithine pathway; putrescine from L-ornithine: step 1/1.
CC -!- SUBUNIT: Homodimer (By similarity). Only the dimer is catalytically
CC active, as the active sites are constructed of residues from both
CC monomers (By similarity). {ECO:0000250|UniProtKB:P08432,
CC ECO:0000250|UniProtKB:P11926}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08432}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC {ECO:0000305}.
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DR EMBL; AJ243276; CAB45689.1; -; mRNA.
DR EMBL; CU329670; CAB59684.1; -; Genomic_DNA.
DR EMBL; D89177; BAA13839.1; -; mRNA.
DR PIR; T37671; T37671.
DR RefSeq; NP_594665.1; NM_001020094.2.
DR AlphaFoldDB; Q9UQW9; -.
DR SMR; Q9UQW9; -.
DR BioGRID; 279301; 13.
DR STRING; 4896.SPAC144.04c.1; -.
DR iPTMnet; Q9UQW9; -.
DR MaxQB; Q9UQW9; -.
DR PaxDb; Q9UQW9; -.
DR PRIDE; Q9UQW9; -.
DR EnsemblFungi; SPAC144.04c.1; SPAC144.04c.1:pep; SPAC144.04c.
DR GeneID; 2542855; -.
DR KEGG; spo:SPAC144.04c; -.
DR PomBase; SPAC144.04c; spe1.
DR VEuPathDB; FungiDB:SPAC144.04c; -.
DR eggNOG; KOG0622; Eukaryota.
DR HOGENOM; CLU_026444_1_2_1; -.
DR InParanoid; Q9UQW9; -.
DR OMA; SFFVCDL; -.
DR PhylomeDB; Q9UQW9; -.
DR Reactome; R-SPO-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-SPO-351143; Agmatine biosynthesis.
DR Reactome; R-SPO-351202; Metabolism of polyamines.
DR UniPathway; UPA00535; UER00288.
DR PRO; PR:Q9UQW9; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004586; F:ornithine decarboxylase activity; ISO:PomBase.
DR GO; GO:0015940; P:pantothenate biosynthetic process; ISO:PomBase.
DR GO; GO:0033387; P:putrescine biosynthetic process from ornithine; ISM:PomBase.
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.
PE 2: Evidence at transcript level;
KW Cytoplasm; Decarboxylase; Lyase; Polyamine biosynthesis;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..432
FT /note="Ornithine decarboxylase"
FT /id="PRO_0000149908"
FT ACT_SITE 377
FT /note="Proton donor; shared with dimeric partner"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 229
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 266
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 296..299
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 341..342
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07805"
FT BINDING 378
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P07805"
FT BINDING 407
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT SITE 226
FT /note="Stacks against the aromatic ring of pyridoxal
FT phosphate and stabilizes reaction intermediates"
FT /evidence="ECO:0000250|UniProtKB:P00860"
FT MOD_RES 98
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT CONFLICT 116
FT /note="F -> L (in Ref. 3; BAA13839)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="L -> P (in Ref. 3; BAA13839)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 432 AA; 47843 MW; F91BD81073970AC9 CRC64;
MPAIMEKNML VSESLRTTEL LGHVKPIDSV VTWSSPGSSR QAIGEAFKNT IEEIERAAVR
GEPADSDAFF VADLNGVYRQ LLRWHAKLPR VQPFYAVKCN PDPKVLALLN KFGTGFDCAS
KGELEQILGL GVSPDRIVYA NPCKAITYVR YAASKGINLM TFDNADELYK VKQHHPNSRL
LLRISTDDSN SLCRLSLKFG ASLDDTGKLL DIAKSLELNV VGVSFHVGSG SYDPSAFLDA
IQRSRQVFDQ GLERGFNFDL LDIGGGFMND SFDGVADLIR SALDTYFDPS IRVISEPGRF
FVSSSFTLAV NVIAKRKLDD EEKVMYYVND GVYGSLNCIL FDHQHPVARV LKCGSRFVYN
DLVGTGQHRC FIWGPTCDSL DVIANDAHLP YELNVGDWIY FEDAGAYTVA AASCFNGFKT
SRIVYLDTDI LD
