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Database: UniProt
Entry: D4F2I4_EDWTA
LinkDB: D4F2I4_EDWTA
Original site: D4F2I4_EDWTA 
ID   D4F2I4_EDWTA            Unreviewed;       714 AA.
AC   D4F2I4;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Lysine decarboxylase, inducible {ECO:0000313|EMBL:EFE24011.1};
DE            EC=4.1.1.18 {ECO:0000313|EMBL:EFE24011.1};
GN   Name=cadA {ECO:0000313|EMBL:EFE24011.1};
GN   ORFNames=EDWATA_00934 {ECO:0000313|EMBL:EFE24011.1};
OS   Edwardsiella tarda ATCC 23685.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=500638 {ECO:0000313|EMBL:EFE24011.1, ECO:0000313|Proteomes:UP000003692};
RN   [1] {ECO:0000313|EMBL:EFE24011.1, ECO:0000313|Proteomes:UP000003692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23685 {ECO:0000313|EMBL:EFE24011.1,
RC   ECO:0000313|Proteomes:UP000003692};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC       {ECO:0000256|ARBA:ARBA00010671}.
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:EFE24011.1}.
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DR   EMBL; ADGK01000038; EFE24011.1; -; Genomic_DNA.
DR   RefSeq; WP_005282982.1; NZ_GG739633.1.
DR   AlphaFoldDB; D4F2I4; -.
DR   SMR; D4F2I4; -.
DR   GeneID; 60779409; -.
DR   HOGENOM; CLU_014292_3_0_6; -.
DR   Proteomes; UP000003692; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0008923; F:lysine decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd00615; Orn_deC_like; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.90.100.10; Orn/Lys/Arg decarboxylase, C-terminal domain; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR005308; OKR_de-COase_N.
DR   InterPro; IPR011193; Orn/lys/arg_de-COase.
DR   InterPro; IPR000310; Orn/Lys/Arg_deCO2ase_major_dom.
DR   InterPro; IPR008286; Prn/Lys/Arg_de-COase_C.
DR   InterPro; IPR036633; Prn/Lys/Arg_de-COase_C_sf.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR45229:SF3; BIODEGRADATIVE ARGININE DECARBOXYLASE; 1.
DR   PANTHER; PTHR45229; CONSTITUTIVE ORNITHINE DECARBOXYLASE; 1.
DR   Pfam; PF01276; OKR_DC_1; 1.
DR   Pfam; PF03711; OKR_DC_1_C; 1.
DR   Pfam; PF03709; OKR_DC_1_N; 1.
DR   PIRSF; PIRSF009393; Orn_decarb; 1.
DR   SUPFAM; SSF55904; Ornithine decarboxylase C-terminal domain; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00703; OKR_DC_1; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:EFE24011.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR009393-1}.
FT   DOMAIN          362..376
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS00703"
FT   MOD_RES         367
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009393-1"
SQ   SEQUENCE   714 AA;  81022 MW;  02114B31DEDD1D19 CRC64;
     MNIIAILNHM GVYFKEEPIR ELHKALEAQN FQIVYPNDRE DLLKLIDNNA RLCGVIFDWD
     TYNLDLCRDI SEMNEHLPVY AFANTHSTLD VSLSDLRLNV EFFEYALGAA EDIALKIRQS
     TDAYVDEILP PLTKALFNYV KEGKYTFCTP GHMGGTAFQK SPVGSLFYDF YGANAMKSDI
     SISVSELGSL LDHTGPHKEA EEYIARTFNA ERSYMVTNGT STANKIVGMY SAPAGSTIMI
     DRNCHKSLTH LMMMSDVTPI YFRPTRNAYG ILGGIPKSEF ARETIEERVK NTPNATWPVH
     AVVTNSTYDG LFYNAEYIKK TLDVKSIHFD SAWVPYTNFS PIYKGLCGMS GDRVEGKVIY
     ETQSTHKLLA AFSQASMIHV KGDINEETFN EAFMMHTSTS PHYGIVASIE TAAAMMKGNA
     GKRLINGSIE RAIRFRKEIK RLRSESDGWF FDVWQPEHID EAKCWNLDPK ESWHGFKDID
     ENHMFLDPIK VTLLTPGMKE DGTMADTGIP ASIVAKYLDE HGIIVEKTGP YNLLFLFSIG
     IDKTKAMSLL RGLTDFKRAY DLNLRVKNML PSLYREDPEF YENMRIQELA QGIHALIQHH
     NLPDLMYRAF EVLPTMVMNP HNAFQMELRG QTEEVYLEEM IGKVNANMIL PYPPGVPLVM
     PGEMLTEESR PVLEFLQMLC EIGAHYPGFE TDIHGAYRQA DGRYTVKVLK TEQK
//
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