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Database: UniProt
Entry: H5V4H1_ATLHE
LinkDB: H5V4H1_ATLHE
Original site: H5V4H1_ATLHE 
ID   H5V4H1_ATLHE            Unreviewed;       712 AA.
AC   H5V4H1;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Inducible lysine decarboxylase {ECO:0000313|EMBL:GAB52879.1};
GN   Name=cadA {ECO:0000313|EMBL:GAB52879.1};
GN   ORFNames=EH105704_09_01040 {ECO:0000313|EMBL:GAB52879.1};
OS   Atlantibacter hermannii NBRC 105704.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Atlantibacter.
OX   NCBI_TaxID=1115512 {ECO:0000313|EMBL:GAB52879.1, ECO:0000313|Proteomes:UP000010297};
RN   [1] {ECO:0000313|EMBL:GAB52879.1, ECO:0000313|Proteomes:UP000010297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 105704 {ECO:0000313|EMBL:GAB52879.1,
RC   ECO:0000313|Proteomes:UP000010297};
RA   Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Escherichia hermannii NBRC 105704.";
RL   Submitted (FEB-2012) 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:GAB52879.1}.
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DR   EMBL; BAFF01000009; GAB52879.1; -; Genomic_DNA.
DR   RefSeq; WP_002436989.1; NZ_BAFF01000009.1.
DR   AlphaFoldDB; H5V4H1; -.
DR   eggNOG; COG1982; Bacteria.
DR   Proteomes; UP000010297; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
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   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR009393-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010297}.
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   712 AA;  80942 MW;  E3E1DA7E076BAC14 CRC64;
     MNCIAIMNHM GVYFKEAPVA ELHKALEKQG FRLVYPNDRE DLLKLIENNA RLCGVIFDWD
     KYNLELCKEI SKFNEYMPVY AFANTYSTLD VSLNDLRMQV RFFEYALGAA EEIAAKIKQS
     TDEYIDTILP PLTRALFKYA REGKYTFCTP GHMGGTAFQK SPVGCLFYDF FGPNTMKSDI
     SISVSELGSL LDHSGPHKEA EEYIARVFNA DRSYMVTNGT STANKIVGMY AAHAGSTVLI
     DRNCHKSLTH LMMMTDITPI YLRPTRNAYG ILGGIPQDEF QRETLARRVN ATPGATWPSH
     AVITNSTYDG LLYNTDFIKE TLDVKSIHFD SAWVPYTNFH PVYQGKCGMS GKRIDGKVIF
     ETQSTHKLLA AFSQASMIHV KGDINEATFN ENYMMHTTTS PHYGIVASTE TAAAMMKGNA
     GKRLIDASIQ RAIKFRKEIK RLRNECDGWF FDIWQPDHID QAECWPLRSD SAWHGFHNID
     NDHMYLDPIK VTILTPGMGK DGRMEPFGIP ASLVAKYLDE HGIIVEKTGP YNLLFLFSIG
     IDKTKALSLL RALTEFKRAF DLNLRVKNML PSLYQEAPEF YETMRIQELA ENIHRLVERH
     NLPDLMYRAF DVLPTMIMTP YHAFQQELRG NVEEVLLDEC IGRVNANMIL PYPPGVPLVM
     PGEMITEESR PILEFLQLLC ETGAHYPGFE TDIHGAYRQP DGRYVVKVLK DK
//
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