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Database: UniProt
Entry: Q57RN4_SALCH
LinkDB: Q57RN4_SALCH
Original site: Q57RN4_SALCH 
ID   Q57RN4_SALCH            Unreviewed;       732 AA.
AC   Q57RN4;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   SubName: Full=Ornithine decarboxylase isozyme, inducible {ECO:0000313|EMBL:AAX64627.1};
GN   Name=speF {ECO:0000313|EMBL:AAX64627.1};
GN   OrderedLocusNames=SCH_0721 {ECO:0000313|EMBL:AAX64627.1};
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314 {ECO:0000313|EMBL:AAX64627.1, ECO:0000313|Proteomes:UP000000538};
RN   [1] {ECO:0000313|EMBL:AAX64627.1, ECO:0000313|Proteomes:UP000000538}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67 {ECO:0000313|EMBL:AAX64627.1,
RC   ECO:0000313|Proteomes:UP000000538};
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.Y., Wang H.S.,
RA   Lee Y.S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
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; AE017220; AAX64627.1; -; Genomic_DNA.
DR   RefSeq; WP_001539477.1; NC_006905.1.
DR   AlphaFoldDB; Q57RN4; -.
DR   KEGG; sec:SCH_0721; -.
DR   HOGENOM; CLU_014292_3_0_6; -.
DR   Proteomes; UP000000538; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004586; F:ornithine decarboxylase activity; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd00615; Orn_deC_like; 1.
DR   Gene3D; 3.40.50.220; -; 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; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR027568; ODC_inducible.
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; IPR027464; Ornithine_deCO2ase_N.
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   NCBIfam; TIGR04301; ODC_inducible; 1.
DR   PANTHER; PTHR45229; CONSTITUTIVE ORNITHINE DECARBOXYLASE; 1.
DR   PANTHER; PTHR45229:SF1; INDUCIBLE 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; SSF52172; CheY-like; 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|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR009393-1}.
FT   DOMAIN          350..364
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS00703"
FT   MOD_RES         355
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009393-1"
SQ   SEQUENCE   732 AA;  82508 MW;  49B90E61DB8A8CCE CRC64;
     MSELKIAVSR HCPDCFSTHR NIVNVDESRF IDVAAIVLSI DDIEHGKLDE IDATGYGIPV
     FVATHDEGRV PPEYLPRISG VFEYNESRTA FYGRQLETAA SHYETQLRPP FFRALVDYVN
     QGNSAFDCPG HQGGEFFRRH PAGNQFVEYF GETLFRSDLC NADVAMGDLL IHEGAPCIAQ
     QHAAKVFNAD KTYFVLNGTS SSNKVVLNAL LTPGDLVLFD RNNHKSNHHG ALLQAGATPV
     YLETARNPYG FIGGIDAHCF EEDYLRELIS EVAPQRAREA RPFRLAVIQL GTYDGTIYNA
     RQVVDKIGHL CDYILFDSAW VGYEQFIPMM ADCSPLLLEL NENDPGILVT QSVHKQQAGF
     SQTSQIHKKD SHIKGQSRYV PHKRMNNAFM MHASTSPFYP LFAALDVNAK MHEGVSGRNM
     WMDCVVNGID ARKLILENCH HIRPFVPELI DGKPWQSYPT SEIASDLRFF HFVPGEHWHA
     FEGYAEHQYF VDPCKLLLTT PGINAASGEY EDFGVPATIL ANFLRENGVV PEKCDLNSIL
     FLLTPAEDMA KLQQLVALLA RFEKLLEADA PLAEVLPSIY KQHEARYADY TLRQLCQEMH
     DLYARHNVKQ LQKEMFRKSH FPKVSMNPQE ANYAYLRGEV ELVRLPEAEG RIAAEGALPY
     PPGVLCVVPG EIWGGSVLRY FSALEEGINL LPGFAPELQG VYIEEHDGRK QVWCYVIKPR
     DAQRSLLKEE KL
//
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