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Database: UniProt
Entry: A0A1F6IBR0_9BACT
LinkDB: A0A1F6IBR0_9BACT
Original site: A0A1F6IBR0_9BACT 
ID   A0A1F6IBR0_9BACT        Unreviewed;       372 AA.
AC   A0A1F6IBR0;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Ornithine decarboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A3D74_03805 {ECO:0000313|EMBL:OGH19993.1};
OS   Candidatus Levybacteria bacterium RIFCSPHIGHO2_02_FULL_37_13.
OC   Bacteria; Candidatus Levybacteria.
OX   NCBI_TaxID=1798602 {ECO:0000313|EMBL:OGH19993.1, ECO:0000313|Proteomes:UP000177483};
RN   [1] {ECO:0000313|EMBL:OGH19993.1, ECO:0000313|Proteomes:UP000177483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR600183-50};
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:OGH19993.1}.
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DR   EMBL; MFNZ01000028; OGH19993.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F6IBR0; -.
DR   STRING; 1798602.A3D74_03805; -.
DR   Proteomes; UP000177483; 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   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50}.
FT   DOMAIN          24..261
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          262..348
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
FT   ACT_SITE        321
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         47
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ   SEQUENCE   372 AA;  41575 MW;  D8C0AAD47554DFA1 CRC64;
     MKLNKQIINK SNQFKTPFLL VDLKQVSKHY NNIKKNLSGV EVFYSMKAND HPRIVETLVK
     ENASFDITSE RELNSLNKNS LSSKKITCLN PIKSPEFLKR LFENKITIMA YDSFDEVDKI
     ARYAPGSKLV LRIVVDNEGS DWPLTKKYGV NPAEALPLLK YALGKKLQPI GLTFHVGSQC
     RNKNNWVNAL FVCETLWALA KKENIHFNFL SLGGGLPIQH DRPIPALEDI GKGIKKMLSN
     NFKSADSPLR VAIEPGRAIV GDSAIMVTSV IGKAKRGSEN WLYVDTGVFN GFMETIDGFT
     YDIKTIKNTA IKKFTIGGPS CDSVDIPFKN VVLEDVKIGD KIYVLNAGAY TTVYASTFNG
     FEIPKTYFLS DD
//
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