ID   A0A176YF50_9BRAD        Unreviewed;       380 AA.
AC   A0A176YF50;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=ornithine decarboxylase {ECO:0000256|ARBA:ARBA00034138};
DE            EC=4.1.1.17 {ECO:0000256|ARBA:ARBA00034138};
GN   ORFNames=AYJ54_22745 {ECO:0000313|EMBL:OAF05261.1};
OS   Bradyrhizobium centrolobii.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1505087 {ECO:0000313|EMBL:OAF05261.1, ECO:0000313|Proteomes:UP000076959};
RN   [1] {ECO:0000313|EMBL:OAF05261.1, ECO:0000313|Proteomes:UP000076959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BR 10245 {ECO:0000313|EMBL:OAF05261.1,
RC   ECO:0000313|Proteomes:UP000076959};
RA   Simoes-Araujo J.L.Sr., Barauna A.C., Silva K., Zilli J.E.;
RT   "Draft Genome Sequence of the Strain BR 10245 (Bradyrhizobium sp.) isolated
RT   from nodules of Centrolobium paraense.";
RL   Submitted (MAR-2016) 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}.
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:OAF05261.1}.
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DR   EMBL; LUUB01000080; OAF05261.1; -; Genomic_DNA.
DR   RefSeq; WP_063704777.1; NZ_LUUB01000080.1.
DR   AlphaFoldDB; A0A176YF50; -.
DR   STRING; 1505087.AYJ54_22745; -.
DR   OrthoDB; 9802147at2; -.
DR   Proteomes; UP000076959; 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}.
FT   DOMAIN          29..262
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          263..358
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
FT   ACT_SITE        328
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         51
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ   SEQUENCE   380 AA;  41577 MW;  73310ABDC654EA5D CRC64;
     MTERIREFLR NRRTEGLDTE PCLVVDLDVV RDNYQSFAKA LPDSRVFYAV KANPAPEVLA
     LLASMGSCFD TATVAEIEMA LAAGATPDRV SFGNTIKKER DIARAFALGI RLFAVDCAAE
     VEKVARAAPG AKVFCRILYD CAGAEWPLSR KFGCDPEMAV EVLDVAKRLG LEPCGISFHV
     GSQQRKVKAW DRALAMASQV FRDCAERGIN LSMVNMGGGF PTKYMKDVPP VVTYGRSIFR
     ALRKHFGNQI PETIIEPGRG MVGNAGIIES EVVLISKKSD EDEVRWVYLD IGKFGGLAET
     MDESIRYAIR TPHDGADMTP CVLAGPTCDS ADVLYEKNPY PLPVTLEIGD KVLIEGTGAY
     TSTYSSVAFN GIPPLKTYHI
//