ID DCOR_CANAL Reviewed; 473 AA. AC P78599; A0A1D8PCA2; P78592; Q5ABD8; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2017, sequence version 2. DT 04-NOV-2026, entry version 136. DE RecName: Full=Ornithine decarboxylase; DE Short=ODC; DE EC=4.1.1.17; GN Name=SPE1; Synonyms=ORD1; OrderedLocusNames=CAALFM_C100740CA; GN ORFNames=CaO19.13453, CaO19.6032; OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes; OC Debaryomycetaceae; Candida. OX NCBI_TaxID=237561; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9392083; RX DOI=10.1002/(sici)1097-0061(199711)13:14<1383::aid-yea189>3.0.co;2-m; RA McNemar M.D., Gorman J.A., Buckley H.R.; RT "Isolation and sequence of the gene encoding ornithine decarboxylase, SPE1, RT from Candida albicans by complementation of a spe1 delta strain of RT Saccharomyces cerevisiae."; RL Yeast 13:1383-1389(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 26555; RX PubMed=9294258; DOI=10.1007/s002940050254; RA Lopez M.C., Garcia S., Ruiz-Herrera J., Dominguez A.; RT "The ornithine decarboxylase gene from Candida albicans. Sequence analysis RT and expression during dimorphism."; RL Curr. Genet. 32:108-114(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=15123810; DOI=10.1073/pnas.0401648101; RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., RA Scherer S.; RT "The diploid genome sequence of Candida albicans."; RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004). RN [4] RP GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52; RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D., RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M., RA Chibana H., Nantel A., Magee P.T.; RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned RT on the eight chromosomes."; RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97; RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.; RT "Assembly of a phased diploid Candida albicans genome facilitates allele- RT specific measurements and provides a simple model for repeat and indel RT structure."; RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013). 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=L-ornithine + H(+) = putrescine + CO2; 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}. 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; U85005; AAC49877.1; -; Genomic_DNA. DR EMBL; X94994; CAA64451.1; -; Genomic_DNA. DR EMBL; CP017623; AOW25771.1; -; Genomic_DNA. DR RefSeq; XP_718994.2; XM_713901.2. DR AlphaFoldDB; P78599; -. DR SMR; P78599; -. DR FunCoup; P78599; 1539. DR STRING; 237561.P78599; -. DR PaxDb; 237561-P78599; -. DR EnsemblFungi; C1_00740C_A-T; C1_00740C_A-T-p1; C1_00740C_A. DR GeneID; 3639327; -. DR KEGG; cal:CAALFM_C100740CA; -. DR CGD; CAL0000182839; SPE1. DR VEuPathDB; FungiDB:C1_00740C_A; -. DR eggNOG; KOG0622; Eukaryota. DR HOGENOM; CLU_026444_1_1_1; -. DR InParanoid; P78599; -. DR OMA; AAEHIAC; -. DR OrthoDB; 5034579at2759; -. DR UniPathway; UPA00535; UER00288. DR PRO; PR:P78599; -. DR Proteomes; UP000000559; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0004586; F:ornithine decarboxylase activity; IGI:CGD. DR GO; GO:0006596; P:polyamine biosynthetic process; IGI:CGD. DR GO; GO:0009446; P:putrescine biosynthetic process; IBA:GO_Central. DR CDD; cd00622; PLPDE_III_ODC; 1. DR FunFam; 3.20.20.10:FF:000005; Ornithine decarboxylase; 1. DR Gene3D; 3.20.20.10; Alanine racemase; 1. DR Gene3D; 2.40.37.10; Lyase, Ornithine Decarboxylase, Chain A, domain 1; 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 3: Inferred from homology; KW Cytoplasm; Decarboxylase; Lyase; Polyamine biosynthesis; KW Pyridoxal phosphate; Reference proteome. FT CHAIN 1..473 FT /note="Ornithine decarboxylase" FT /id="PRO_0000149905" FT ACT_SITE 417 FT /note="Proton donor; shared with dimeric partner" 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:P07805" FT BINDING 240 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000250|UniProtKB:P07805" FT BINDING 277 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000250|UniProtKB:P07805" FT BINDING 315 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000250|UniProtKB:P07805" FT BINDING 316 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000250|UniProtKB:P07805" FT BINDING 367 FT /ligand="L-ornithine" FT /ligand_id="ChEBI:CHEBI:46911" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P07805" FT BINDING 367 FT /ligand="putrescine" FT /ligand_id="ChEBI:CHEBI:326268" FT /evidence="ECO:0000250|UniProtKB:P07805" FT BINDING 368 FT /ligand="L-ornithine" FT /ligand_id="ChEBI:CHEBI:46911" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P07805" FT BINDING 368 FT /ligand="putrescine" FT /ligand_id="ChEBI:CHEBI:326268" FT /evidence="ECO:0000250|UniProtKB:P07805" FT BINDING 417 FT /ligand="L-ornithine" FT /ligand_id="ChEBI:CHEBI:46911" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P07805" FT BINDING 417 FT /ligand="putrescine" FT /ligand_id="ChEBI:CHEBI:326268" FT /evidence="ECO:0000250|UniProtKB:P07805" FT BINDING 418 FT /ligand="L-ornithine" FT /ligand_id="ChEBI:CHEBI:46911" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P07805" FT BINDING 418 FT /ligand="putrescine" FT /ligand_id="ChEBI:CHEBI:326268" FT /evidence="ECO:0000250|UniProtKB:P07805" FT BINDING 447 FT /ligand="L-ornithine" FT /ligand_id="ChEBI:CHEBI:46911" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P07805" FT BINDING 447 FT /ligand="putrescine" FT /ligand_id="ChEBI:CHEBI:326268" FT /evidence="ECO:0000250|UniProtKB:P07805" FT BINDING 447 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000250|UniProtKB:P07805" FT SITE 237 FT /note="Stacks against the aromatic ring of pyridoxal FT phosphate and stabilizes reaction intermediates" FT /evidence="ECO:0000250|UniProtKB:P00860" FT MOD_RES 106 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000250|UniProtKB:P11926" FT CONFLICT 95 FT /note="I -> S (in Ref. 2; CAA64451)" FT /evidence="ECO:0000305" FT CONFLICT 164 FT /note="D -> N (in Ref. 2; CAA64451)" FT /evidence="ECO:0000305" FT CONFLICT 228 FT /note="G -> S (in Ref. 2; CAA64451)" FT /evidence="ECO:0000305" FT CONFLICT 305 FT /note="L -> S (in Ref. 1; AAC49877 and 2; CAA64451)" FT /evidence="ECO:0000305" FT CONFLICT 342 FT /note="N -> H (in Ref. 2; CAA64451)" FT /evidence="ECO:0000305" FT CONFLICT 399..401 FT /note="Missing (in Ref. 2; CAA64451)" FT /evidence="ECO:0000305" SQ SEQUENCE 473 AA; 52931 MW; 99F6B8FF2A9A3DE6 CRC64; MKHTIIENEP EIKLQNDLNH HIEISPNTKT TNGTTTTTTT LNVNKTLKAI DLIETSIKNH ISTIDHENCL PNDEDSFFVC DLGEIINSVN QWQQILPMVQ PYYAVKCNSN PQILTTLSEL GVNFDCASKN EIDLVLSLGI HQAHERIIYA NPCKTNSFIR HAADENVNLT TVDNVHELYK LAKFHPHCKI LIRLITDDST AQCQLSTKFG CDLNTAIGEI LPKAKELGLQ VHGVAFHVGS GAKDFSSIYQ AIKDSRILFD EMLSMGFTPK LLDIGGGFER ETFPQSSQMV KFALEKFFPI EFSQLNEIKF IAEPGRFMVA NAFTLITHII ARRDLPTGGN NNNNDMTPSA MLYINDGVYG NLNCILFDHQ TPKVYVLTNE NQLFYKQEMM RSLSVNNNNN NNNKTDGFKF SIWGPTCDGL DCVSSLAKLS KNVQVGDWLF FENVGAYTSC ASTKFNGLSS GETKTLYVNS NEE //