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Database: UniProt
Entry: E0SIF1_DICD3
LinkDB: E0SIF1_DICD3
Original site: E0SIF1_DICD3 
ID   E0SIF1_DICD3            Unreviewed;       411 AA.
AC   E0SIF1;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   SubName: Full=Diaminopimelate decarboxylase {ECO:0000313|EMBL:ADM97832.1};
DE            EC=4.1.1.20 {ECO:0000313|EMBL:ADM97832.1};
GN   Name=acsE {ECO:0000313|EMBL:ADM97832.1};
GN   OrderedLocusNames=Dda3937_02853 {ECO:0000313|EMBL:ADM97832.1};
OS   Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=198628 {ECO:0000313|EMBL:ADM97832.1, ECO:0000313|Proteomes:UP000006859};
RN   [1] {ECO:0000313|EMBL:ADM97832.1, ECO:0000313|Proteomes:UP000006859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3937 {ECO:0000313|EMBL:ADM97832.1,
RC   ECO:0000313|Proteomes:UP000006859};
RX   PubMed=21217001; DOI=10.1128/JB.01513-10;
RA   Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA   Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA   Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA   Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA   Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA   Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA   Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA   Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA   Blattner F.R., Keen N.T., Perna N.T.;
RT   "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL   J. Bacteriol. 193:2076-2077(2011).
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; CP002038; ADM97832.1; -; Genomic_DNA.
DR   RefSeq; WP_013317293.1; NC_014500.1.
DR   AlphaFoldDB; E0SIF1; -.
DR   STRING; 198628.Dda3937_02853; -.
DR   GeneID; 9733052; -.
DR   KEGG; ddd:Dda3937_02853; -.
DR   PATRIC; fig|198628.6.peg.1621; -.
DR   eggNOG; COG0019; Bacteria.
DR   HOGENOM; CLU_026444_0_3_6; -.
DR   OMA; LCTPNDT; -.
DR   OrthoDB; 9802147at2; -.
DR   Proteomes; UP000006859; Chromosome.
DR   GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042861; P:achromobactin biosynthetic process; IGI:ASAP.
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; 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   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   Lyase {ECO:0000313|EMBL:ADM97832.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006859}.
FT   DOMAIN          33..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   411 AA;  45360 MW;  1A1FACBF79D9D8DC CRC64;
     MVNLPQHVHD VIVLLQQQHT DPLAAFVYDL TALRQHVSEV MAALPPGVEL YYAIKANSEK
     PILDAIAPLV HGFEISSGGE IARVAGCGTR KPFVFSGPGK LDSDFDLALE QGVEAVHVES
     RHEIARLQQR ARQHGVVQPV FIRVNPELAS SLTSKLAMAG TPTPFGMDEA DLADAVRDVD
     NASHLQLKGF HVHAMSHQMV VARHQQLLDL YLTRWPQWKA LSAHPQHITH LNVGGGIGVP
     YLTPERFDWP ALCDYLRTRL AQQPDAPIVR FEPGRFISAY CGYYAIEVLD KKRSHGKHFL
     VCRGGTHQFR LPVAQGHDHP VIHLPLTSAP TTGETRDWTV VGQLCTPKDV LSRDQRLTDV
     NIGDLLVLPL AGAYGYNISH ADFLCHPRPG QYFTTEDGMT TDAAGVVSRV E
//
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