ID A0KHI2_AERHH Unreviewed; 710 AA.
AC A0KHI2;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Lysine decarboxylase, constitutive {ECO:0000313|EMBL:ABK38124.1};
DE EC=4.1.1.18 {ECO:0000313|EMBL:ABK38124.1};
GN OrderedLocusNames=AHA_1192 {ECO:0000313|EMBL:ABK38124.1};
OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK38124.1, ECO:0000313|Proteomes:UP000000756};
RN [1] {ECO:0000313|EMBL:ABK38124.1, ECO:0000313|Proteomes:UP000000756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 /
RC KCTC 2358 / NCIMB 9240 / NCTC 8049
RC {ECO:0000313|Proteomes:UP000000756};
RX PubMed=16980456; DOI=10.1128/JB.00621-06;
RA Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.,
RA Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL J. Bacteriol. 188:8272-8282(2006).
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC {ECO:0000256|ARBA:ARBA00010671}.
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DR EMBL; CP000462; ABK38124.1; -; Genomic_DNA.
DR RefSeq; WP_011705110.1; NC_008570.1.
DR RefSeq; YP_855733.1; NC_008570.1.
DR AlphaFoldDB; A0KHI2; -.
DR STRING; 380703.AHA_1192; -.
DR EnsemblBacteria; ABK38124; ABK38124; AHA_1192.
DR KEGG; aha:AHA_1192; -.
DR PATRIC; fig|380703.7.peg.1199; -.
DR eggNOG; COG1982; Bacteria.
DR HOGENOM; CLU_014292_3_0_6; -.
DR OrthoDB; 9761189at2; -.
DR Proteomes; UP000000756; 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:ABK38124.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR009393-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000756}.
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 710 AA; 80091 MW; CFA44E1033F429F3 CRC64;
MNIIAILNHL GVFFKEEPIR QLQASLERKG FEVVYPVDVA DLLKLIEKNP RVCGAIFDWD
KYSLGLCKEI HDRNEKLPIF AFANDQSTLD IHLTDLRLNV HFFEYRLGMA DDIALKMGQA
TQEYQDAILP PFTKALFKYV EEGKYTFCTP GHMGGTAFQM SPAGSIFYDF YGPNAFKADV
SISMPELGSL LDHSGPHKEA EEYIARTFNA DRSYIVTNGT STANKIVGMY SAPAGSTVLV
DRNCHKSLTH LMMMNDVTPL YFRPTRNAYG ILGGIPQSEF SRETIAAKVA ATPGAQAPRY
AVITNSTYDG LLYNTGFIKE ALDTPYIHFD SAWVPYTNFS PIYEGKCGMS GEAMPGKVFY
ETQSTHKLLA AFSQASMIHI KGDVEEETFN EAFMMHTSTS PQYGIVASTE ISAAMMRGNT
GKRLIKDSID RAISFRKEIK RLREQSEGWF FDVWQPDDID TVECWKLDPK DDWHGFKDID
DDHMYLDPIK VTLLTPGMGR NGQLLENGIP ASLVSKFLDE RGIVVEKTGP YNLLFLFSIG
IDQSKAMQLL RALTEFKRGY DLNLTIKSIL PSLYREDPSF YEGMRIQELA QRIHELTSKY
RLPELMFKAF DVLPEMKMTP HAAWQQELAG NVVEVPLRDM VDRISANMIL PYPPGVPLVL
PGEMVTQDSL PVLEFLEMLC EIGAHYPGFE TDIHGLYRQA DGSYTVKVLR
//
