ID   Q9UVG2_PHAND            Unreviewed;       445 AA.
AC   Q9UVG2; Q0UX71;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 102.
DE   RecName: Full=ornithine decarboxylase {ECO:0000256|ARBA:ARBA00034138};
DE            EC=4.1.1.17 {ECO:0000256|ARBA:ARBA00034138};
GN   Name=odc1 {ECO:0000313|EMBL:CAB56523.1};
OS   Phaeosphaeria nodorum (Glume blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=13684 {ECO:0000313|EMBL:CAB56523.1};
RN   [1] {ECO:0000313|EMBL:CAB56523.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LAW 95 {ECO:0000313|EMBL:CAB56523.1};
RA   Bailey A.M.;
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAB56523.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LAW 95 {ECO:0000313|EMBL:CAB56523.1};
RX   PubMed=10799502; DOI=10.1074/jbc.275.19.14242;
RA   Bailey A., Mueller E., Bowyer P.;
RT   "Ornithine decarboxylase of Stagonospora (Septoria) nodorum is required for
RT   virulence toward wheat.";
RL   J. Biol. Chem. 275:14242-14247(2000).
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:0000256|ARBA:ARBA00034037};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR600183-50};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC       L-ornithine pathway; putrescine from L-ornithine: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00034115}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       {ECO:0000256|ARBA:ARBA00008872, ECO:0000256|RuleBase:RU003737}.
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DR   EMBL; AJ249387; CAB56523.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9UVG2; -.
DR   PHI-base; PHI:177; -.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0006596; P:polyamine biosynthetic process; IEA:InterPro.
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   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50}.
FT   DOMAIN          71..301
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          302..411
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
FT   ACT_SITE        383
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         95
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ   SEQUENCE   445 AA;  48937 MW;  D59CA6642C75C00B CRC64;
     MAPSAITTTE EYQTLKDSLQ SLNSQTLGSV ENHGAWKSKQ LIGSALKSRV EAIDHDSCDV
     GDEDAFFIAD LGEVYRQHLR WKKNLARVKP HYAVKCNPDT QVLRLMSELG MGFDCASKNE
     IETVLKLGVD PARIIYAQPC KTKSYVRYAA NSGVKQMTFD NADELYKTKQ LFPDAELYLR
     ILTDDSGSLC RLSQKFGASL DTTAELLELA HKLELNVVGV AFHVGSGASD PKAFIKAVQD
     ARFVFDQAAA FGFDMHTLDV GGGFTGDITF EPMAAVLSAS LDEYFPPHIR VIGEPGRYYV
     STAFTIACHV IARRTVADAT LGTTSYMLYL NDGVYGNFSS IIFDHQHPVP RVLKSGNDVL
     YDVRTSGYDT PSQVEYSIWG PTCDGIDIIS SSCSFPELLD VGDWLYFEDM GAYTKCSATK
     FNGFTDSHDV VYVCSEPGAK ALMGM
//