DCOR_NEUCR
ID DCOR_NEUCR Reviewed; 484 AA.
AC P27121; Q7S7C1;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Ornithine decarboxylase;
DE Short=ODC;
DE EC=4.1.1.17;
GN Name=spe-1; ORFNames=B13M13.130, NCU01271;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=74-ORS-6a / FGSC 4200;
RX PubMed=1530878; DOI=10.1128/mcb.12.1.347-359.1992;
RA Williams L.J., Barnett G.R., Ristow J.L., Pitkin J., Perriere M.,
RA Davis R.H.;
RT "Ornithine decarboxylase gene of Neurospora crassa: isolation, sequence,
RT and polyamine-mediated regulation of its mRNA.";
RL Mol. Cell. Biol. 12:347-359(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator.
CC {ECO:0000305}.
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DR EMBL; M68969; AAA33604.1; -; mRNA.
DR EMBL; M68970; AAA33605.1; -; Genomic_DNA.
DR EMBL; L16920; AAA33614.1; -; Genomic_DNA.
DR EMBL; BX842618; CAE76122.1; -; Genomic_DNA.
DR EMBL; CM002240; EAA31513.1; -; Genomic_DNA.
DR PIR; A42065; A42065.
DR RefSeq; XP_960749.1; XM_955656.3.
DR AlphaFoldDB; P27121; -.
DR SMR; P27121; -.
DR STRING; 5141.EFNCRP00000004012; -.
DR EnsemblFungi; EAA31513; EAA31513; NCU01271.
DR GeneID; 3876899; -.
DR KEGG; ncr:NCU01271; -.
DR VEuPathDB; FungiDB:NCU01271; -.
DR HOGENOM; CLU_026444_1_2_1; -.
DR InParanoid; P27121; -.
DR OMA; SFFVCDL; -.
DR SABIO-RK; P27121; -.
DR UniPathway; UPA00535; UER00288.
DR Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004586; F:ornithine decarboxylase activity; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cytoplasm; Decarboxylase; Lyase; Polyamine biosynthesis;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..484
FT /note="Ornithine decarboxylase"
FT /id="PRO_0000149906"
FT ACT_SITE 422
FT /note="Proton donor; shared with dimeric partner"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 245
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 282
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 315..318
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT BINDING 381..382
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07805"
FT BINDING 423
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P07805"
FT BINDING 452
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11926"
FT SITE 242
FT /note="Stacks against the aromatic ring of pyridoxal
FT phosphate and stabilizes reaction intermediates"
FT /evidence="ECO:0000250|UniProtKB:P00860"
FT MOD_RES 114
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P11926"
SQ SEQUENCE 484 AA; 53301 MW; 3554F4315EA44A6F CRC64;
MVMPTVVSDR MGTIDFIDYT NNHVFSKCQT DSLNTVNNGS LKHDDYLHGL ANGKLVAKQM
IGDALRQRVE SIDSEFCEPG DEDTFFVADL GEVYRQHLRW KLNLPRVKPF YAVKCHPDER
LLQLLAALGT GFDCASKAEI EQVLRMGVDP SRIIYAQPCK TNSYLRYVAQ QGVRQMTFDN
ADELRKIARL YPDAELFLRI LTDDSSSLCR FSMKFGASLD STDGLLGLAR QLGLNVVGVS
FHVGSGASDP TAFLKAVQDA HVVFQQAAAY GYSLKTLDVG GGFCSDDSFE QMANVLRAAL
DEYFPAHTGV NLIAEPGRYY ASSAFTLACN IIARRTIQDG SAVSVSDSSS MSDDGSVNNG
DARYMVYVND GLYGNFSSIM FDHQHPVAKI LRAGGRTMYN SVAAHESSAE DAIEYSIWGP
TCDGIDRITE SIRFREILDV GDWLYFEDMG AYTKCSATTF NGFSNEHDVI YVCSEPGAMA
LLGL
