ID B8E6G0_SHEB2 Unreviewed; 391 AA.
AC B8E6G0;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=ornithine decarboxylase {ECO:0000256|ARBA:ARBA00034138};
DE EC=4.1.1.17 {ECO:0000256|ARBA:ARBA00034138};
GN OrderedLocusNames=Sbal223_0489 {ECO:0000313|EMBL:ACK45023.1};
OS Shewanella baltica (strain OS223).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=407976 {ECO:0000313|EMBL:ACK45023.1, ECO:0000313|Proteomes:UP000002507};
RN [1] {ECO:0000313|Proteomes:UP000002507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS223 {ECO:0000313|Proteomes:UP000002507};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ovchinnikova G., Brettar I., Rodrigues J., Konstantinidis K.,
RA Tiedje J.;
RT "Complete sequence of chromosome of Shewanella baltica OS223.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-ornithine = CO2 + putrescine; 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:ARBA00034037};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR600183-50};
CC -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC L-ornithine pathway; putrescine from L-ornithine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00034115}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC {ECO:0000256|ARBA:ARBA00008872, ECO:0000256|RuleBase:RU003737}.
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DR EMBL; CP001252; ACK45023.1; -; Genomic_DNA.
DR RefSeq; WP_012586648.1; NC_011663.1.
DR AlphaFoldDB; B8E6G0; -.
DR KEGG; sbp:Sbal223_0489; -.
DR HOGENOM; CLU_026444_1_3_6; -.
DR Proteomes; UP000002507; Chromosome.
DR GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0004586; F:ornithine decarboxylase activity; IEA:RHEA.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:InterPro.
DR CDD; cd00622; PLPDE_III_ODC; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR022643; De-COase2_C.
DR InterPro; IPR022657; De-COase2_CS.
DR InterPro; IPR022644; De-COase2_N.
DR InterPro; IPR022653; De-COase2_pyr-phos_BS.
DR InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR InterPro; IPR002433; Orn_de-COase.
DR InterPro; IPR029066; PLP-binding_barrel.
DR PANTHER; PTHR11482; ARGININE/DIAMINOPIMELATE/ORNITHINE DECARBOXYLASE; 1.
DR PANTHER; PTHR11482:SF6; ORNITHINE DECARBOXYLASE 1-RELATED; 1.
DR Pfam; PF02784; Orn_Arg_deC_N; 1.
DR Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR PRINTS; PR01179; ODADCRBXLASE.
DR PRINTS; PR01182; ORNDCRBXLASE.
DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS00878; ODR_DC_2_1; 1.
DR PROSITE; PS00879; ODR_DC_2_2; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:ACK45023.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50}.
FT DOMAIN 40..274
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 275..369
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 339
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 61
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 391 AA; 43994 MW; 2796D304413882C7 CRC64;
MSQFQSIDVA DYYDMDTFKR IEAFAKDKAT PFVVIDTSII AKQYDDMVNS FPYANVYYAV
KANPAAEILS LLKDKGSNFD IASIYELDMV MNVGVTTDRV SYGNTIKKRQ DVRAFYERGV
RMYASDSEAD LRMIAEEAPG SRIYVRILTE GTDTADWPLS RKFGCQNEMA YELLVLAQEL
GLEPFGISFH VGSQQRDIGA WDSAIGKVKS IFDRLRDEHS ITLKMINMGG GFPANYIDKT
NQLGVYAEQI THFLKEDFGD DLPQIILEPG RSLISNAGIL VSEVVLISKK SYTALERWVF
TDVGKFSGLI ETMDEAIKFP IYTDRQGELD KCVIAGPTCD SADIMYEHYS YGLPNDLAIG
DRMYWLTAGA YTTTYSAVCF NGFPPLKDYY L
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