ID   B2VHY3_ERWT9            Unreviewed;       719 AA.
AC   B2VHY3;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Lysine decarboxylase {ECO:0000313|EMBL:CAO95953.1};
DE            EC=4.1.1.18 {ECO:0000313|EMBL:CAO95953.1};
GN   Name=cadA {ECO:0000313|EMBL:CAO95953.1};
GN   OrderedLocusNames=ETA_09070 {ECO:0000313|EMBL:CAO95953.1};
OS   Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS   4357 / Et1/99).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=465817 {ECO:0000313|EMBL:CAO95953.1, ECO:0000313|Proteomes:UP000001726};
RN   [1] {ECO:0000313|EMBL:CAO95953.1, ECO:0000313|Proteomes:UP000001726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99
RC   {ECO:0000313|Proteomes:UP000001726};
RX   PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA   Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA   Geider K.;
RT   "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT   bacterium in the genus Erwinia.";
RL   Environ. Microbiol. 10:2211-2222(2008).
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}.
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DR   EMBL; CU468135; CAO95953.1; -; Genomic_DNA.
DR   RefSeq; WP_012440655.1; NC_010694.1.
DR   AlphaFoldDB; B2VHY3; -.
DR   STRING; 465817.ETA_09070; -.
DR   KEGG; eta:ETA_09070; -.
DR   eggNOG; COG1982; Bacteria.
DR   HOGENOM; CLU_014292_3_0_6; -.
DR   OrthoDB; 9761189at2; -.
DR   Proteomes; UP000001726; Chromosome.
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:CAO95953.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR009393-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001726}.
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   719 AA;  80933 MW;  BC86F1FDD443CB11 CRC64;
     MNIIAIMGPN HVFYKDEPVR ELDAALKQQG FHTVYPQGAE DLLKLIEHNP RICGVVFDWD
     EYSLDLCSEI NQLNEYLPLY AFINTHSTMD VGINEMRMAI WFFEYALNAA EEIALRIRQS
     TEEYVDTITP PLTKALFNYV KEGKTTFCTP GHMAGTAFQK SPVGSLFYDF FGANTLKADI
     SISVSELGSL LDHTGPHLEA EEYIARTFGA EQSYMVTNGT STSNKIVGMY AAAAGSTVLI
     DRNCHKSLTH LLMMSDIIPI WLKPTRNALG ILGGIPKREF SKESIALKVS QTPRAGWPVH
     AVITNSTYDG LLYSTQFIKE TLEVPSIHFD SAWVPYTNFH PIYRGLSGMS GERTPGKVIY
     ETQSTHKLLA AFSQASLIHI KGDYDEQTFN EAYMMHTTTS PNYAIVASIE TAAAMLRGNS
     GRRLINRSVE RALHFRREVQ RLREESDGWF FDIWQPDGVD EPECWAIQPG GEEWHGFRDA
     DADHMYLDPI KVTILTPGMS EMGEMAEEGI PAALVAKFLD ERGVVVEKTG PYNLLFLFSI
     GIDKTKAMSV LRGLTEFKRA YDLNLRVKNM LPDLYAQDPD FYRNMRIQTL AQGIHSLIRQ
     HDLPRLMLQA FAMLPEMKLT PHQMFQQQVQ GNVETVDISR LVGRVSANMI LPYPPGVPLV
     MPGEMITEES RPVLDFLLML CTIGRHYPGF ETDIHGATLT EEGQYLVRVL KQAGENEPV
//