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Database: UniProt
Entry: A4YBQ4_SHEPC
LinkDB: A4YBQ4_SHEPC
Original site: A4YBQ4_SHEPC 
ID   A4YBQ4_SHEPC            Unreviewed;       720 AA.
AC   A4YBQ4;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=Ornithine decarboxylase {ECO:0000313|EMBL:ABP77387.1};
DE            EC=4.1.1.17 {ECO:0000313|EMBL:ABP77387.1};
GN   OrderedLocusNames=Sputcn32_3679 {ECO:0000313|EMBL:ABP77387.1};
OS   Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=319224 {ECO:0000313|EMBL:ABP77387.1};
RN   [1] {ECO:0000313|EMBL:ABP77387.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CN-32 {ECO:0000313|EMBL:ABP77387.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella putrefaciens CN-32.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC       {ECO:0000256|ARBA:ARBA00010671}.
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DR   EMBL; CP000681; ABP77387.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4YBQ4; -.
DR   STRING; 319224.Sputcn32_3679; -.
DR   KEGG; spc:Sputcn32_3679; -.
DR   eggNOG; COG1982; Bacteria.
DR   HOGENOM; CLU_014292_3_0_6; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004586; F:ornithine 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; 3.40.50.220; -; 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: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; 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   Lyase {ECO:0000313|EMBL:ABP77387.1};
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   720 AA;  81068 MW;  3437675C745740B2 CRC64;
     MKSLKVAASL SVRSCFDIDR EVVNVLTTDF CDVGAAVVSV DDVRNGIVEK IKNTGLKLPI
     FVSVCCEETF PDDVCSSITG VFELCGDNTD FYGKQVETAV NKYEQALLPP FFGTLKKYVE
     MGNSTFACPG HQGGQFFRKH PVGRQFFDFF GETIFRADMC NADVKLGDLL IHEGAPLDAQ
     KYAAKVFNAD KTYFVLNGTS SSNKVATNAL LAKGDLVLFD RNNHKSNHHG ALIQAGATPI
     YLETARNPFG FIGGIDAHCF QESYLREQIR EVAPERADEK RPFRLAIIQL GTYDGTIYNA
     RQVVDRIGHL CDYILFDSAW VGYEQFIPMM NDCSPLLLEL TPEDPGIIVT QSVHKQQAGF
     SQTSQIHKKD KHIKGQARYC NHKRFNNAFM MHASTSPFYP LFAALDVNAK MHEGASGRYL
     WREAVKAGIE ARKLLLKKCK YIKPFVPTMI DGRLWQEYET EQMADDLRFF EFEPGQKWHS
     FDGYEKGQYF VDPCKFLLTT PGIDAETGKY TEFGIPATIL ANFLRENNII PEKCDLNSIL
     FLMTPAEDMA KMQHLVSQIS RFEKLVDEDA PLSEVLPNVY NANKARYKDY TIRQLCQEMH
     NLYVSHDVKQ LQKEMFRKAH FPTKVMDPQE ANLEFIRGKV ELVPLSQIEG RIAAEGALPY
     PPGVLCMVPG EIWGGAVQRY FLALEEGINL LPGFSPELQG VYLENTAEGK IQALGYVLAK
//
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