DCOR_CANAL
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 03-AUG-2022, entry version 126.
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; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; 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=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; 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 STRING; 237561.P78599; -.
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 OrthoDB; 725914at2759; -.
DR UniPathway; UPA00535; UER00288.
DR PRO; PR:P78599; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004586; F:ornithine decarboxylase activity; IGI:CGD.
DR GO; GO:0006596; P:polyamine biosynthetic process; IGI:CGD.
DR GO; GO:0033387; P:putrescine biosynthetic process from ornithine; IBA:GO_Central.
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 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 240
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 277
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 313..316
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 367..368
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07805"
FT BINDING 418
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
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:P11926"
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
