ID A0A1I4VF41_9GAMM Unreviewed; 418 AA.
AC A0A1I4VF41;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Diaminopimelate decarboxylase {ECO:0000313|EMBL:SFM99802.1};
GN ORFNames=SAMN05216289_10229 {ECO:0000313|EMBL:SFM99802.1};
OS Dokdonella immobilis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dokdonella.
OX NCBI_TaxID=578942 {ECO:0000313|EMBL:SFM99802.1, ECO:0000313|Proteomes:UP000198575};
RN [1] {ECO:0000313|EMBL:SFM99802.1, ECO:0000313|Proteomes:UP000198575}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7659 {ECO:0000313|EMBL:SFM99802.1,
RC ECO:0000313|Proteomes:UP000198575};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOVF01000002; SFM99802.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4VF41; -.
DR STRING; 578942.SAMN05216289_10229; -.
DR OrthoDB; 9802241at2; -.
DR Proteomes; UP000198575; Unassembled WGS sequence.
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; 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000198575}.
FT DOMAIN 57..302
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 303..396
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 369
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 79
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 418 AA; 44271 MW; 670B8CF794020DAA CRC64;
MTDPTQSVPA APAAAWSARQ PWPRNAGGEW LIGGQPLSQV VDSVGGTPCY LYDRARLGAR
VDQLRATLPD AVRLHYAMKA NPMPALVCHM AGLVDGIDVA SRGELRVALD SGMPATRISF
AGPGKSALEL QQSVAAGILV NLESFRELDI LASASAAWGL PARVAVRVNL PFELRASGMK
MSGGARPFGI DAERVPEMLA AIAARGLAFE GFHLYAGSQN LRPAAIIEAQ TLSYELVLGW
LDHCPAAPRT LNLGGGFGIP YTLNDTPLDI EPVAAHLERL VERARRDMPA AHLALELGRY
LVGEAGLYVT RVVDRKVSRG QVFLVVDGGM HQHLAASGNF GQVMRRNYPV AINRGGAGRE
TASVVGPLCT PLDLLADRAE LAVADVGDLV VVFQSGAYGR SASPREFLGH ADVAEALV
//
