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Database: UniProt
Entry: A0A085U984_YERRU
LinkDB: A0A085U984_YERRU
Original site: A0A085U984_YERRU 
ID   A0A085U984_YERRU        Unreviewed;       720 AA.
AC   A0A085U984;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   18-JUN-2025, entry version 57.
DE   RecName: Full=ornithine decarboxylase {ECO:0000256|ARBA:ARBA00034138};
DE            EC=4.1.1.17 {ECO:0000256|ARBA:ARBA00034138};
GN   Name=speF {ECO:0000313|EMBL:SUQ00352.1};
GN   ORFNames=CSF007_2345 {ECO:0000313|EMBL:CEK26252.1}, NCTC10476_01635
GN   {ECO:0000313|EMBL:SUQ00352.1};
OS   Yersinia ruckeri.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Yersiniaceae; Yersinia.
OX   NCBI_TaxID=29486 {ECO:0000313|EMBL:CEK26252.1};
RN   [1] {ECO:0000313|EMBL:CEK26252.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CSF007-82 {ECO:0000313|EMBL:CEK26252.1};
RA   Nelson M.C., LaPatra S.E., Welch T.J., Graf J.;
RT   "Complete Genome Sequence of Yersinia ruckeri Strain CSF007-82, Etiologic
RT   Agent of Red Mouth Disease in Salmonid Fish.";
RL   Genome Announc. 3:1-2(2015).
RN   [2] {ECO:0000313|EMBL:SUQ00352.1, ECO:0000313|Proteomes:UP000255169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC10476 {ECO:0000313|EMBL:SUQ00352.1,
RC   ECO:0000313|Proteomes:UP000255169};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-ornithine + H(+) = putrescine + CO2; Xref=Rhea:RHEA:22964,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:46911,
CC         ChEBI:CHEBI:326268; EC=4.1.1.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00049127};
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; LN681231; CEK26252.1; -; Genomic_DNA.
DR   EMBL; UHJG01000001; SUQ00352.1; -; Genomic_DNA.
DR   RefSeq; WP_004720425.1; NZ_VDHI01000017.1.
DR   AlphaFoldDB; A0A085U984; -.
DR   STRING; 29486.UGYR_12145; -.
DR   GeneID; 66878239; -.
DR   KEGG; yrb:UGYR_12145; -.
DR   PATRIC; fig|29486.44.peg.828; -.
DR   eggNOG; COG1982; Bacteria.
DR   OrthoDB; 9761189at2; -.
DR   Proteomes; UP000255169; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004586; F:ornithine decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:TreeGrafter.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd00615; Orn_deC_like; 1.
DR   FunFam; 3.40.640.10:FF:000008; Lysine decarboxylase, inducible; 1.
DR   FunFam; 3.90.1150.10:FF:000032; Ornithine decarboxylase SpeF; 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   NCBIfam; NF010092; PRK13578.1; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:CEK26252.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR009393-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000255169}.
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;  81065 MW;  F83C44C1F1F7F038 CRC64;
     MKKLNIAASA SAISCFETQR EVVDVLHTDF TDISAVVLSV QDINNGVIES IHSLGFNIPI
     FAAVCCEEEL NNDVLPSLNG VFELCGDNTD FYGKQLESAA EKYENELLPP FFNTLTKYVE
     MGNSTFACPG HQGGQFFRKH PAGRQFFDFY GETIFRSDMC NADVKLGDLL IHEGAPCDAQ
     KHAAKVFNAD KTYFVLNGTS ASNKVATNAI LARGDLVLFD RNNHKSNHHG ALIQAGATPV
     YLETARNPFG FIGGIDAHCF EEKYLREQIR SVSPERADAP RPFRLAIIQL GTYDGTIYNA
     RQVVDKIGHL CDYILFDSAW VGYEQFIPMM KDCSPLLLEL NENDPGIIVT QSVHKQQAGF
     SQTSQIHKKD KHIKGQDRYC NHKRFNNAFM LHASTSPFYP LFAALDVNAK MHEGESGRRM
     WLECVKNGIE ARKMLLNTCT MIKPFVPDTV DGKPWQEYDT DAMAQDLRFF NFIPGEKWHA
     FEGYETSQYF VDPCKLLLTT PGIDTNTGKY THSGIPATIL ANFLRENGIV PEKCDLNSIL
     FLLTPAEDLA KMQHLVAQIA RFERFIEEDA LLCDVLPTVY RNNEARYKDY TIGRLCQEMH
     DLYVSYDVKQ LQKEMFRKQY FPKVVMNPQD ANIEFVRGNA ELVPLCKAEG RIAAEGALPY
     PPGVLCVVPG EVWGGAAQRY FLALEESINL LPGFAPELQG VYLQVDEDGW NRAYGYMMKQ
//
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