ID U2Y5M7_9SPHN Unreviewed; 401 AA.
AC U2Y5M7;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=ornithine decarboxylase {ECO:0000256|ARBA:ARBA00034138};
DE EC=4.1.1.17 {ECO:0000256|ARBA:ARBA00034138};
GN ORFNames=NT2_02_05100 {ECO:0000313|EMBL:GAD48426.1};
OS Caenibius tardaugens NBRC 16725.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Caenibius.
OX NCBI_TaxID=1219035 {ECO:0000313|EMBL:GAD48426.1, ECO:0000313|Proteomes:UP000016568};
RN [1] {ECO:0000313|EMBL:GAD48426.1, ECO:0000313|Proteomes:UP000016568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 16725 {ECO:0000313|EMBL:GAD48426.1,
RC ECO:0000313|Proteomes:UP000016568};
RA Isaki S., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Novosphingobium tardaugens NBRC 16725.";
RL Submitted (SEP-2013) 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:GAD48426.1}.
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DR EMBL; BASZ01000002; GAD48426.1; -; Genomic_DNA.
DR RefSeq; WP_021689333.1; NZ_CP034179.1.
DR AlphaFoldDB; U2Y5M7; -.
DR KEGG; ntd:EGO55_02100; -.
DR eggNOG; COG0019; Bacteria.
DR OrthoDB; 9802147at2; -.
DR Proteomes; UP000016568; 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; IPR022657; De-COase2_CS.
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 SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS00878; ODR_DC_2_1; 1.
DR PROSITE; PS00879; ODR_DC_2_2; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000016568}.
FT DOMAIN 35..266
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 268..350
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 326
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 48
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 401 AA; 43737 MW; 077CEC0BCD6DC902 CRC64;
MYIYPDASAV VRDLAPDEPV ILNRPHAAAR AGRFFAEKFP GKSLYAVKAN PSPDLIEILW
ASGITHYDVA SIAEVRMVRG LLPDATLCFM HPVKTASAIR EAYFDHGVRT FSLDTEEELN
KIVEATKDAA GNVAADLRLC VRLRVSSEYS ELSLASKFGV DLANAAPLLQ ATRQVADWLG
VCFHVGSQAM TPFAYVQALD RVRAAIAQAA VTVDIVDVGG GFPSVYPGME PPPLEDYFAI
IHRHFEALPI AYNAELWCEP GRALCAEYSS LIVKVEKRRG EELYINDGAY GALFDAAHVG
WRFPVKVLDA SRSASEAEFA FYGPTCDDAD YMEGPFMLPG DVVAGDYIEV GMLGAYGCAM
RTAFNGFGRG EVVRVADEPM ASLYRGDRAD PRQSDNVVSL R
//