ID Q7N8H2_PHOLL Unreviewed; 419 AA.
AC Q7N8H2;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Photorhabdus luminescens subsp. laumondii TTO1 complete genome segment 3/17 {ECO:0000313|EMBL:CAE13047.1};
GN OrderedLocusNames=plu0752 {ECO:0000313|EMBL:CAE13047.1};
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01) (Photorhabdus luminescens subsp. laumondii).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265 {ECO:0000313|EMBL:CAE13047.1, ECO:0000313|Proteomes:UP000002514};
RN [1] {ECO:0000313|Proteomes:UP000002514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01
RC {ECO:0000313|Proteomes:UP000002514};
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
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|RuleBase:RU003737}.
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DR EMBL; BX571861; CAE13047.1; -; Genomic_DNA.
DR RefSeq; WP_011145126.1; NC_005126.1.
DR AlphaFoldDB; Q7N8H2; -.
DR STRING; 243265.plu0752; -.
DR GeneID; 24167895; -.
DR KEGG; plu:plu0752; -.
DR eggNOG; COG0019; Bacteria.
DR HOGENOM; CLU_026444_0_3_6; -.
DR Proteomes; UP000002514; Chromosome.
DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:UniProt.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:InterPro.
DR CDD; cd06839; PLPDE_III_Btrk_like; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR017530; DCO2ase_PEP1.
DR InterPro; IPR022643; De-COase2_C.
DR InterPro; IPR022657; De-COase2_CS.
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 NCBIfam; TIGR03099; dCO2ase_PEP1; 1.
DR PANTHER; PTHR43727; DIAMINOPIMELATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43727:SF2; DIAMINOPIMELATE DECARBOXYLASE 1, CHLOROPLASTIC-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; 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:UP000002514}.
FT DOMAIN 52..302
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 303..397
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 370
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 76
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 419 AA; 46143 MW; EF3D0478DFF36CD4 CRC64;
MNIENRITQK SLSMKIAETF VIKDDCLEIG GIPLTRLETQ IGQTPFFAYS RKHIDQQVCL
LRKYLPEKIS IHYAIKANPF VPLIHHLSQK IEGFDVASAN EMALALNTGV SPEDISFAGP
GKTDTELKRA IAAQVLLNVE SLNELRRIQI LSEKLGLCAR VSLRINPDYN LNSSGMKMGG
GPRQFGMDVV YVPEALMFIR DYPDSLVFEG FQIYPGSQNL CAEHLIEAQN KALNLVIELS
HSAPSPVRRF NLGGGFGVPY FQGNTELNIT EVGNAMHKLV ERAEKFLPEV EIILELGRYL
VASSGIYVTK IVERKISHDM TFLVTDGGMN HHLSASGNLG QLIRRNYPAI IGNKIKGEKR
ETVNIVGPLC TPLDILVHQG DMSVATPGDL VVIFQSGAYG LSASPNNFLS QTNAVEVLV
//