ID   A0A074TH84_9RHOB        Unreviewed;       381 AA.
AC   A0A074TH84;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=ornithine decarboxylase {ECO:0000256|ARBA:ARBA00034138};
DE            EC=4.1.1.17 {ECO:0000256|ARBA:ARBA00034138};
GN   ORFNames=DL1_03765 {ECO:0000313|EMBL:KEP69515.1};
OS   Thioclava dalianensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Thioclava.
OX   NCBI_TaxID=1185766 {ECO:0000313|EMBL:KEP69515.1, ECO:0000313|Proteomes:UP000027725};
RN   [1] {ECO:0000313|EMBL:KEP69515.1, ECO:0000313|Proteomes:UP000027725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DLFJ1-1 {ECO:0000313|EMBL:KEP69515.1,
RC   ECO:0000313|Proteomes:UP000027725};
RA   Lai Q., Shao Z.;
RT   "The draft genome sequence of Thioclava dalianensis DLFJ1-1.";
RL   Submitted (MAR-2014) 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:KEP69515.1}.
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DR   EMBL; JHEH01000013; KEP69515.1; -; Genomic_DNA.
DR   RefSeq; WP_038066366.1; NZ_JHEH01000013.1.
DR   AlphaFoldDB; A0A074TH84; -.
DR   STRING; 1185766.SAMN05216224_10926; -.
DR   eggNOG; COG0019; Bacteria.
DR   OrthoDB; 9802147at2; -.
DR   Proteomes; UP000027725; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0006596; P:polyamine biosynthetic process; IEA:InterPro.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027725}.
FT   DOMAIN          37..263
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          266..355
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
FT   ACT_SITE        327
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         52
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ   SEQUENCE   381 AA;  40348 MW;  186F6C426D0715DF CRC64;
     MELSDPIWAS PREIIRARRP QHPISVFAPS ALQATAQHFL HGFPGLVTYA VKANPEPMVI
     ENLVAAGITG FDVASPAEIA LIRSLAPGSA LHYHNPVRSR DEIACAIAAE VTSWSVDSQS
     ELDKLRAQGL VPGSEIAVRF KLPVAGAAYD FGSKFGATEA QAVQLLAQAA ALGFRPSLTF
     HPGTQCTDPA AWDTYIRAAA SIARAAGVTL ARLNLGGGFP SHRAQGPAPA LDEIFARIDQ
     AVETAFGAAR PALVCEPGRG LVADSVTHIA CVKALRDGRD VFLNDGVYGA LTELPQIGLL
     ERIEVIAPDG RPRRAPAYPR VVFGPTCDSL DRLPGEMALP GDLAEGDYIL FHGLGAYSGV
     TNTRFNGFGQ LETLTAMRLT D
//