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Database: UniProt
Entry: A0A094EBG0_9PEZI
LinkDB: A0A094EBG0_9PEZI
Original site: A0A094EBG0_9PEZI 
ID   A0A094EBG0_9PEZI        Unreviewed;       425 AA.
AC   A0A094EBG0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   13-SEP-2023, entry version 29.
DE   RecName: Full=Ornithine decarboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=V496_00612 {ECO:0000313|EMBL:KFY69025.1};
OS   Pseudogymnoascus sp. VKM F-4515 (FW-2607).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420909 {ECO:0000313|EMBL:KFY69025.1, ECO:0000313|Proteomes:UP000029302};
RN   [1] {ECO:0000313|EMBL:KFY69025.1, ECO:0000313|Proteomes:UP000029302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4515 (FW-2607) {ECO:0000313|Proteomes:UP000029302};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       {ECO:0000256|ARBA:ARBA00008872, ECO:0000256|RuleBase:RU003737}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFY69025.1}.
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DR   EMBL; JPJY01000094; KFY69025.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094EBG0; -.
DR   STRING; 1420909.A0A094EBG0; -.
DR   HOGENOM; CLU_026444_1_2_1; -.
DR   OrthoDB; 48358at2759; -.
DR   Proteomes; UP000029302; Unassembled WGS sequence.
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; IPR022644; De-COase2_N.
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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000029302}.
FT   DOMAIN          57..278
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          279..377
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
SQ   SEQUENCE   425 AA;  47210 MW;  806589894166AC43 CRC64;
     MSVATLGPTP IQLSHIREPS LVEQTILERI ENDQQTKLDQ HANLRHEGDR AFFVVDLGKV
     YKQHQRWTKE LRRVQPYYGS SVLTSYKLGV GFDCASIDEI KLVLNLAPEP TRVIFSNPCK
     SDYSIRFAAD ARVRMMSFDN LDELEKIKKY HPGADLLIRI FASDPTALVH LESKYGASLE
     STITLLRRAF ALELNVVGVS FHVGSGAGDV AAIGQAIKDS SLVLEEAKSV GFNPHILNVG
     GGFQDCNFEL ISGALRTALQ THIPKNIAII AEPGRYFARS AYTLACTVIG RRQVHNGSMD
     MIYQNDGVYG NFLNVIIEKE AISPSIVFLI NQQERQLTTR VYSIWGPTCD STDCVNPISR
     FGTEIMVGDW LIYKNMGGSV PKTPCRMGFL TNLAYTTSTS TNFNGFSSLY PTVYICSEAT
     VMHLF
//
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