ID F6AD41_PSEF1 Unreviewed; 399 AA.
AC F6AD41;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Diaminopimelate decarboxylase {ECO:0000313|EMBL:AEF22351.1};
DE EC=4.1.1.20 {ECO:0000313|EMBL:AEF22351.1};
GN OrderedLocusNames=Psefu_2385 {ECO:0000313|EMBL:AEF22351.1};
OS Pseudomonas fulva (strain 12-X).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=743720 {ECO:0000313|EMBL:AEF22351.1, ECO:0000313|Proteomes:UP000000686};
RN [1] {ECO:0000313|EMBL:AEF22351.1, ECO:0000313|Proteomes:UP000000686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12-X {ECO:0000313|Proteomes:UP000000686};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Pagani I., Davenport K., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Lcollab F.I.,
RA Woyke T.;
RT "Complete sequence of Pseudomonas fulva 12-X.";
RL Submitted (APR-2011) 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; CP002727; AEF22351.1; -; Genomic_DNA.
DR RefSeq; WP_013791479.1; NC_015556.1.
DR AlphaFoldDB; F6AD41; -.
DR STRING; 743720.Psefu_2385; -.
DR KEGG; pfv:Psefu_2385; -.
DR eggNOG; COG0019; Bacteria.
DR HOGENOM; CLU_026444_0_3_6; -.
DR OrthoDB; 9802147at2; -.
DR Proteomes; UP000000686; Chromosome.
DR GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:InterPro.
DR CDD; cd06843; PLPDE_III_PvsE_like; 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; IPR000183; Orn/DAP/Arg_de-COase.
DR InterPro; IPR002433; Orn_de-COase.
DR InterPro; IPR029066; PLP-binding_barrel.
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 Lyase {ECO:0000313|EMBL:AEF22351.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000000686}.
FT DOMAIN 32..279
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 280..372
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 345
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 55
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 399 AA; 43561 MW; 2DDEBF90E6A3341E CRC64;
MDKLPASVLD AIEQAHSRAA DPLAVFAYDL DALAQHVREV MAALPAGVEL FYAIKANSEA
PILRTLAPLV DGFEISSGGE IERLQAASSD RPFVFSGPGK LDSDFRAALS QGVAAIHVES
LGEIERLQRI AVELGRVQPV FIRINPELPT TLSSRLAMGG TATPFGLDEA EVPEAVKRVE
ASSHLRLQGF HVHAMSHQQQ VERHEQLLDL YLERWAQWKA LANRPETVTH LNVGGGIGVD
YLSGERFDWP RLCRHLERRL GALADAPVVR FEPGRFISAY CGYYAIEVLD SKSSHGQHFL
ICRGGTHQFR LPVAQGHDHP VIHLPAAGRE PSGVSRPFSV VGQLCTPKDV LSRGRQLVDP
AVGDLLVLPM AGAYGYNISH ADFLCHPRPE QVFVGRGDG
//
