ID   DCOR_ECOLI              Reviewed;         711 AA.
AC   P21169; Q2M9M8;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   03-AUG-2022, entry version 162.
DE   RecName: Full=Constitutive ornithine decarboxylase;
DE            EC=4.1.1.17;
GN   Name=speC; OrderedLocusNames=b2965, JW5482;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Barroso L.A., Moore R., Wright J., Patel T., Boyle S.M.;
RT   "Analysis and sequence of the speC (ornithine decarboxylase) gene of
RT   Escherichia coli.";
RL   Submitted (MAY-1990) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC       L-ornithine pathway; putrescine from L-ornithine: step 1/1.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA66174.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAA69133.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; M33766; AAA66174.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U28377; AAA69133.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC76002.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77028.1; -; Genomic_DNA.
DR   PIR; I60729; I60729.
DR   RefSeq; NP_417440.4; NC_000913.3.
DR   RefSeq; WP_001326492.1; NZ_LN832404.1.
DR   AlphaFoldDB; P21169; -.
DR   SMR; P21169; -.
DR   BioGRID; 4262354; 4.
DR   DIP; DIP-10907N; -.
DR   STRING; 511145.b2965; -.
DR   jPOST; P21169; -.
DR   PaxDb; P21169; -.
DR   PRIDE; P21169; -.
DR   EnsemblBacteria; AAC76002; AAC76002; b2965.
DR   EnsemblBacteria; BAE77028; BAE77028; BAE77028.
DR   GeneID; 947457; -.
DR   KEGG; ecj:JW5482; -.
DR   KEGG; eco:b2965; -.
DR   PATRIC; fig|1411691.4.peg.3765; -.
DR   EchoBASE; EB0954; -.
DR   eggNOG; COG1982; Bacteria.
DR   HOGENOM; CLU_014292_3_0_6; -.
DR   InParanoid; P21169; -.
DR   OMA; MKGRSGE; -.
DR   PhylomeDB; P21169; -.
DR   BioCyc; EcoCyc:ORNDECARBOX-BIO-MON; -.
DR   BioCyc; MetaCyc:ORNDECARBOX-BIO-MON; -.
DR   BRENDA; 4.1.1.17; 2026.
DR   UniPathway; UPA00535; UER00288.
DR   PRO; PR:P21169; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR   GO; GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc.
DR   GO; GO:0004586; F:ornithine decarboxylase activity; IDA:EcoCyc.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
DR   GO; GO:0033387; P:putrescine biosynthetic process from ornithine; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IMP:EcoCyc.
DR   CDD; cd00615; Orn_deC_like; 1.
DR   Gene3D; 3.40.50.220; -; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
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   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; SSF52172; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   SUPFAM; SSF55904; SSF55904; 1.
DR   PROSITE; PS00703; OKR_DC_1; 1.
PE   1: Evidence at protein level;
KW   Decarboxylase; Lyase; Pyridoxal phosphate; Reference proteome;
KW   Spermidine biosynthesis.
FT   CHAIN           1..711
FT                   /note="Constitutive ornithine decarboxylase"
FT                   /id="PRO_0000201134"
FT   MOD_RES         347
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   711 AA;  79416 MW;  37E54AC603853C3C CRC64;
     MKSMNIAASS ELVSRLSSHR RVVALGDTDF TDVAAVVITA ADSRSGILAL LKRTGFHLPV
     FLYSEHAVEL PAGVTAVING NEQQWLELES AACQYEENLL PPFYDTLTQY VEMGNSTFAC
     PGHQHGAFFK KHPAGRHFYD FFGENVFRAD MCNADVKLGD LLIHEGSAKD AQKFAAKVFH
     ADKTYFVLNG TSAANKVVTN ALLTRGDLVL FDRNNHKSNH HGALIQAGAT PVYLEASRNP
     FGFIGGIDAH CFNEEYLRQQ IRDVAPEKAD LPRPYRLAII QLGTYDGTVY NARQVIDTVG
     HLCDYILFDS AWVGYEQFIP MMADSSPLLL ELNENDPGIF VTQSVHKQQA GFSQTSQIHK
     KDNHIRGQAR FCPHKRLNNA FMLHASTSPF YPLFAALDVN AKIHEGESGR RLWAECVEIG
     IEARKAILAR CKLFRPFIPP VVDGKLWQDY PTSVLASDRR FFSFEPGAKW HGFEGYAADQ
     YFVDPCKLLL TTPGIDAETG EYSDFGVPAT ILAHYLRENG IVPEKCDLNS ILFLLTPAES
     HEKLAQLVAM LAQFEQHIED DSPLVEVLPS VYNKYPVRYR DYTLRQLCQE MHDLYVSFDV
     KDLQKAMFRQ QSFPSVVMNP QDAHSAYIRG DVELVRIRDA EGRIAAEGAL PYPPGVLCVV
     PGEVWGGAVQ RYFLALEEGV NLLPGFSPEL QGVYSETDAD GVKRLYGYVL K