ID A0A1G2DFJ9_9BACT Unreviewed; 393 AA.
AC A0A1G2DFJ9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=ornithine decarboxylase {ECO:0000256|ARBA:ARBA00034138};
DE EC=4.1.1.17 {ECO:0000256|ARBA:ARBA00034138};
GN ORFNames=A3C93_03470 {ECO:0000313|EMBL:OGZ12346.1};
OS Candidatus Lloydbacteria bacterium RIFCSPHIGHO2_02_FULL_54_17.
OC Bacteria; Candidatus Lloydbacteria.
OX NCBI_TaxID=1798664 {ECO:0000313|EMBL:OGZ12346.1, ECO:0000313|Proteomes:UP000178636};
RN [1] {ECO:0000313|EMBL:OGZ12346.1, ECO:0000313|Proteomes:UP000178636}
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 -!- 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:OGZ12346.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MHLO01000020; OGZ12346.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2DFJ9; -.
DR STRING; 1798664.A3C93_03470; -.
DR Proteomes; UP000178636; 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 36..271
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 272..368
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 338
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 59
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 393 AA; 43391 MW; 4EEBEC4D07076717 CRC64;
MGNKSRPNEL ISADDLARIV AFTKDKATPC LVMDLEKVGE RYDELLQAMP GARIYYALKA
NPLDDVVALL RDRGASFDVA SRFEIDQLLT LNVSPERMSY GNTIKKESDI AYAYQKGIRV
FTTDSRSDVE KLARSAPGAL LNFRLLLDGT GADWPLSKKF GAHPDMLYKL VKFAKKSGLT
PYGISFHVGS QQRDIGQWDS AIALVKYLFD ALASDGINLE SINLGGGLPA QYLKPAQGVA
AYTGSIIQFL NEDFPERKLA LVVEPGRSLV ADAGVIVSEV VMVSKKSDTN RTRWVYLDVG
KFNGLIETTD EAIKYPILFP GRDGKEEWSE VVLAGPTCDS ADILYENYRY KVPNNLKEGE
RVYILTTGAY TMSYSSICFN GFPPLAVHVL PPK
//
