ID DCOR_YEAST Reviewed; 466 AA.
AC P08432; D6VX16;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 08-NOV-2023, entry version 179.
DE RecName: Full=Ornithine decarboxylase;
DE Short=ODC;
DE EC=4.1.1.17 {ECO:0000269|PubMed:6795198};
GN Name=SPE1 {ECO:0000303|PubMed:2669750}; Synonyms=ORD1;
GN OrderedLocusNames=YKL184W {ECO:0000312|SGD:S000001667};
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3038869; DOI=10.1016/s0021-9258(18)61087-7;
RA Fonzi W.A., Sypherd P.S.;
RT "The gene and the primary structure of ornithine decarboxylase from
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 262:10127-10133(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8154185; DOI=10.1002/yea.320091208;
RA Wiemann S., Voss H., Schwager C., Rupp T., Stegemann J., Zimmermann J.,
RA Grothues D., Sensen C., Erfle H., Hewitt N., Banrevi A., Ansorge W.;
RT "Sequencing and analysis of 51.6 kilobases on the left arm of chromosome XI
RT from Saccharomyces cerevisiae reveals 23 open reading frames including the
RT FAS1 gene.";
RL Yeast 9:1343-1348(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=6795198; DOI=10.1016/s0021-9258(18)43247-4;
RA Tyagi A.K., Tabor C.W., Tabor H.;
RT "Ornithine decarboxylase from Saccharomyces cerevisiae. Purification,
RT properties, and regulation of activity.";
RL J. Biol. Chem. 256:12156-12163(1981).
RN [6]
RP PATHWAY.
RX PubMed=6754461;
RA Tabor C.W., Tabor H., Tyagi A.K., Cohn M.S.;
RT "The biochemistry, genetics, and regulation of polyamine biosynthesis in
RT Saccharomyces cerevisiae.";
RL Fed. Proc. 41:3084-3088(1982).
RN [7]
RP SUBUNIT.
RX PubMed=2669750; DOI=10.1016/0006-291x(89)90831-0;
RA Fonzi W.A.;
RT "Biochemical and genetic characterization of the structure of yeast
RT ornithine decarboxylase.";
RL Biochem. Biophys. Res. Commun. 162:1409-1416(1989).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP ACTIVITY REGULATION.
RX PubMed=15538383; DOI=10.1038/sj.emboj.7600473;
RA Palanimurugan R., Scheel H., Hofmann K., Dohmen R.J.;
RT "Polyamines regulate their synthesis by inducing expression and blocking
RT degradation of ODC antizyme.";
RL EMBO J. 23:4857-4867(2004).
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:0000269|PubMed:6795198}.
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:0000269|PubMed:6795198};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:6795198};
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:0000269|PubMed:15538383}.
CC -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC L-ornithine pathway; putrescine from L-ornithine: step 1/1.
CC {ECO:0000305|PubMed:6754461}.
CC -!- SUBUNIT: Homodimer (PubMed:2669750). Only the dimer is catalytically
CC active, as the active sites are constructed of residues from both
CC monomers (By similarity). {ECO:0000250|UniProtKB:P11926,
CC ECO:0000269|PubMed:2669750}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 688 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J02777; AAA34829.1; -; Genomic_DNA.
DR EMBL; X74151; CAA52254.1; -; Genomic_DNA.
DR EMBL; Z28184; CAA82027.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA08982.1; -; Genomic_DNA.
DR PIR; A28437; DCBYO.
DR RefSeq; NP_012737.1; NM_001179750.1.
DR AlphaFoldDB; P08432; -.
DR SMR; P08432; -.
DR BioGRID; 33938; 508.
DR STRING; 4932.YKL184W; -.
DR iPTMnet; P08432; -.
DR PaxDb; 4932-YKL184W; -.
DR PeptideAtlas; P08432; -.
DR EnsemblFungi; YKL184W_mRNA; YKL184W; YKL184W.
DR GeneID; 853651; -.
DR KEGG; sce:YKL184W; -.
DR AGR; SGD:S000001667; -.
DR SGD; S000001667; SPE1.
DR VEuPathDB; FungiDB:YKL184W; -.
DR eggNOG; KOG0622; Eukaryota.
DR GeneTree; ENSGT00950000182995; -.
DR HOGENOM; CLU_026444_1_2_1; -.
DR InParanoid; P08432; -.
DR OMA; SFFVCDL; -.
DR OrthoDB; 48358at2759; -.
DR BioCyc; MetaCyc:YKL184W-MONOMER; -.
DR BioCyc; YEAST:YKL184W-MONOMER; -.
DR BRENDA; 4.1.1.17; 984.
DR Reactome; R-SCE-351143; Agmatine biosynthesis.
DR Reactome; R-SCE-351202; Metabolism of polyamines.
DR UniPathway; UPA00535; UER00288.
DR BioGRID-ORCS; 853651; 1 hit in 10 CRISPR screens.
DR PRO; PR:P08432; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P08432; Protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0004586; F:ornithine decarboxylase activity; IDA:SGD.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IMP:SGD.
DR GO; GO:0009446; P:putrescine biosynthetic process; IMP:SGD.
DR GO; GO:0033387; P:putrescine biosynthetic process from ornithine; IBA:GO_Central.
DR CDD; cd00622; PLPDE_III_ODC; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 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; ARGININE/DIAMINOPIMELATE/ORNITHINE DECARBOXYLASE; 1.
DR PANTHER; PTHR11482:SF6; ORNITHINE DECARBOXYLASE 1-RELATED; 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; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS00878; ODR_DC_2_1; 1.
DR PROSITE; PS00879; ODR_DC_2_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Decarboxylase; Lyase; Polyamine biosynthesis;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..466
FT /note="Ornithine decarboxylase"
FT /id="PRO_0000149909"
FT ACT_SITE 411
FT /note="Proton donor; shared with dimeric partner"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 247
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 286
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 318..321
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 362..363
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07805"
FT BINDING 412
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P07805"
FT BINDING 441
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT SITE 244
FT /note="Stacks against the aromatic ring of pyridoxal
FT phosphate and stabilizes reaction intermediates"
FT /evidence="ECO:0000250|UniProtKB:P00860"
FT MOD_RES 116
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P11926"
SQ SEQUENCE 466 AA; 52285 MW; 2EBD7EE8CFAA67CD CRC64;
MSSTQVGNAL SSSTTTLVDL SNSTVTQKKQ YYKDGETLHN LLLELKNNQD LELLPHEQAH
PKIFQALKAR IGRINNETCD PGEENSFFIC DLGEVKRLFN NWVKELPRIK PFYAVKCNPD
TKVLSLLAEL GVNFDCASKV EIDRVLSMNI SPDRIVYANP CKVASFIRYA ASKNVMKSTF
DNVEELHKIK KFHPESQLLL RIATDDSTAQ CRLSTKYGCE MENVDVLLKA IKELGLNLAG
VSFHVGSGAS DFTSLYKAVR DARTVFDKAA NEYGLPPLKI LDVGGGFQFE SFKESTAVLR
LALEEFFPVG CGVDIIAEPG RYFVATAFTL ASHVIAKRKL SENEAMIYTN DGVYGNMNCI
LFDHQEPHPR TLYHNLEFHY DDFESTTAVL DSINKTRSEY PYKVSIWGPT CDGLDCIAKE
YYMKHDVIVG DWFYFPALGA YTSSAATQFN GFEQTADIVY IDSELD
//
