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Database: UniProt
Entry: A0A074X366_9PEZI
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ID   A0A074X366_9PEZI        Unreviewed;       445 AA.
AC   A0A074X366;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=ornithine decarboxylase {ECO:0000256|ARBA:ARBA00034138};
DE            EC=4.1.1.17 {ECO:0000256|ARBA:ARBA00034138};
GN   ORFNames=M436DRAFT_78013 {ECO:0000313|EMBL:KEQ78179.1};
OS   Aureobasidium namibiae CBS 147.97.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ78179.1, ECO:0000313|Proteomes:UP000027730};
RN   [1] {ECO:0000313|EMBL:KEQ78179.1, ECO:0000313|Proteomes:UP000027730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ78179.1,
RC   ECO:0000313|Proteomes:UP000027730};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA   Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA   Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
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; KL584702; KEQ78179.1; -; Genomic_DNA.
DR   RefSeq; XP_013432458.1; XM_013577004.1.
DR   AlphaFoldDB; A0A074X366; -.
DR   STRING; 1043004.A0A074X366; -.
DR   GeneID; 25416132; -.
DR   HOGENOM; CLU_026444_1_2_1; -.
DR   OrthoDB; 48358at2759; -.
DR   Proteomes; UP000027730; 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; 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.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027730}.
FT   DOMAIN          70..298
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          299..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         93
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ   SEQUENCE   445 AA;  48673 MW;  F2633036F772D8B3 CRC64;
     MAPSAISPTT EHYASLSLKS SYTPRLEESH NGKALSKPMI ARALYQRVQS IDQDTCEPGE
     EDAFFVADMG DIYRQHLRWK KHLNRVKPHY AVKCNPDPQV LRLLAAMGTG FDCASKAEID
     MVLRLGVDPS RIIYAQPCKT KSYVRYAAKQ GVRQMTFDNA DELYKIKDLY PDAELYLRIL
     TDDSASLCRL SLKFGASLDD TGDLLALASK LGLNVVGVAF HVGSGASDPA AFLKAVRDAR
     FVFDQAAALG YDLKTLDVGG GFVSETFDAM AAVLSAALDE YFPPSVRVIG EPGRYYVSSA
     FTIACNVIAR RSVEDKALGL NSYMLYLNDG VYGNFSSIMF DHQHPIPRVL KAANSPASTY
     DAVAAYDANI QSPIEYSIWG PTCDGIDCIS ESWTCAQTLD VGDWLYFEDM GAYTKCSATK
     FNGFSDSHAT VYISSEPGAS ALLGY
//
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