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Database: UniProt
Entry: A0A0M7BA97_9RHOB
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ID   A0A0M7BA97_9RHOB        Unreviewed;       392 AA.
AC   A0A0M7BA97;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, 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   Name=ldc {ECO:0000313|EMBL:CUH38863.1};
GN   ORFNames=JSE7799_01581 {ECO:0000313|EMBL:CUH38863.1};
OS   Jannaschia seosinensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia.
OX   NCBI_TaxID=313367 {ECO:0000313|EMBL:CUH38863.1, ECO:0000313|Proteomes:UP000049455};
RN   [1] {ECO:0000313|EMBL:CUH38863.1, ECO:0000313|Proteomes:UP000049455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7799 {ECO:0000313|EMBL:CUH38863.1,
RC   ECO:0000313|Proteomes:UP000049455};
RA   Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA   Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA   Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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; CYPR01000097; CUH38863.1; -; Genomic_DNA.
DR   RefSeq; WP_055663130.1; NZ_CYPR01000097.1.
DR   AlphaFoldDB; A0A0M7BA97; -.
DR   STRING; 313367.JSE7799_01581; -.
DR   OrthoDB; 9802241at2; -.
DR   Proteomes; UP000049455; Unassembled WGS sequence.
DR   GO; GO:0004586; F:ornithine decarboxylase activity; IEA:UniProtKB-EC.
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   Lyase {ECO:0000313|EMBL:CUH38863.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000049455}.
FT   DOMAIN          41..275
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          276..370
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
FT   ACT_SITE        340
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         64
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ   SEQUENCE   392 AA;  41868 MW;  1F1CED4A10F9A57C CRC64;
     MNAVTGLGRT VSTPEAAAPS RVEAYIAAHD FDRPTLVIDV DAVERQFRAL RAGLGRAHMH
     YAVKANPHDA IVARLVALGS GFDAASRGEI ELVLGHGASP EHVSFGNTIK RASDIRFAHE
     AGITLFAADA EEELEKIAAN APGARVYIRV IVDNPEADWP LSRKFGCACD KVLSLLGCAR
     DLGLVPHGLS FHVGSQTREA RMWTGTLDQV AAIWRRAGEA GFDLQLLNIG GGFPAFYGED
     IQHPTAYAAA VMDLIAERFG DVPEIMAEPG RGLVAEAGAI AAEVLLVSRK SDADLHRWVY
     LDIGRFSGLA ETEGEAIRYQ FATARDGEQA GPCVLAGPSC DSADVLYEKR PVQLPLSLCG
     GDKVVIRNCG AYTSTYSSVG FNGFPPLDTR VI
//
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