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Database: UniProt
Entry: A0A097R5J6_HAFAL
LinkDB: A0A097R5J6_HAFAL
Original site: A0A097R5J6_HAFAL 
ID   A0A097R5J6_HAFAL        Unreviewed;       713 AA.
AC   A0A097R5J6;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Lysine decarboxylase LdcC {ECO:0000313|EMBL:AIU73989.1};
DE            EC=4.1.1.18 {ECO:0000313|EMBL:AIU73989.1};
GN   ORFNames=AT03_17370 {ECO:0000313|EMBL:AIU73989.1};
OS   Hafnia alvei FB1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Hafnia.
OX   NCBI_TaxID=1453496 {ECO:0000313|EMBL:AIU73989.1, ECO:0000313|Proteomes:UP000029986};
RN   [1] {ECO:0000313|EMBL:AIU73989.1, ECO:0000313|Proteomes:UP000029986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB1 {ECO:0000313|EMBL:AIU73989.1,
RC   ECO:0000313|Proteomes:UP000029986};
RX   PubMed=25075225; DOI=10.1186/1757-4749-6-29;
RA   Tan J.Y., Yin W.F., Chan K.G.;
RT   "Gene clusters of Hafnia alvei strain FB1 important in survival and
RT   pathogenesis: a draft genome perspective.";
RL   Gut Pathog. 6:29-29(2014).
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; CP009706; AIU73989.1; -; Genomic_DNA.
DR   RefSeq; WP_025800207.1; NZ_CP009706.1.
DR   AlphaFoldDB; A0A097R5J6; -.
DR   SMR; A0A097R5J6; -.
DR   GeneID; 78451499; -.
DR   KEGG; hav:AT03_17370; -.
DR   PATRIC; fig|1453496.5.peg.3568; -.
DR   eggNOG; COG1982; Bacteria.
DR   HOGENOM; CLU_014292_3_0_6; -.
DR   OrthoDB; 9761189at2; -.
DR   Proteomes; UP000029986; 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:AIU73989.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR009393-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029986}.
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   713 AA;  80440 MW;  1814AF43D1C345C7 CRC64;
     MNIIAILNHM GVYFKEEPIR ELHKALEALD FQIVYPNDRE DLLKLIDNNA RLCGVIFDWD
     TYNLDLCEEI SAMNEHLPVY AFANTHSTLD VSLNDLRLNV EFFEYALGAA QDIAQKIRQS
     TDAYIDEILP PLTKALFNYV KEGKYTFCTP GHMGGTAFQK SPVGSIFYDF FGANAMKSDI
     SISVGELGSL LDHSGPHKEA EEYIARTFNA ERSYMVTNGT STANKIVGMY SAPAGSTVLI
     DRNCHKSLTH LMMMSDITPI YFRPTRNAYG ILGGIPKSEF QHDTIAERVA QTPNATWPVH
     AVVTNSTYDG LLYNTDYIKE ALDVKSIHFD SAWVPYTNFS PIYKGLCGMS GGRVEGKVIY
     ETQSTHKLLA AFSQASMIHV KGDINEETFN EAYMMHTSTS PHYGIVASTE TAAAMMKGNA
     GKRLINGSIE RAIRFRKEIK RLNSESEGWF FDVWQPEGID EAKCWPLDSK DSWHGFKDID
     NDHMYLDPIK VTLLTPGMQK DGSMADTGIP ASIVSKYLDE HGIIVEKTGP YNLLFLFSIG
     IDKTKALSLL RALTEFKRSY DLNLRVKNML PSLYREDPEF YENMRIQDLA QGIHALIQHH
     NLPDLMYRAF EVLPTMVMNP HAAFQKELRG QTEEVYLEEM IGKVNANMIL PYPPGVPLVM
     PGEMLTEESR PVLEFLQMLC EIGAHYPGFE TDIHGAYRQA DGRYTVKVIK DQK
//
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