DCOS_ECOLI
ID DCOS_ECOLI Reviewed; 732 AA.
AC P24169;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Inducible ornithine decarboxylase;
DE EC=4.1.1.17 {ECO:0000269|PubMed:1939141};
GN Name=speF {ECO:0000303|PubMed:1939141}; OrderedLocusNames=b0693, JW0680;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS AN ORNITHINE DECARBOXYLASE,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND OPERON.
RC STRAIN=K12 / 3000/ DR112;
RX PubMed=1939141; DOI=10.1016/s0021-9258(18)54798-0;
RA Kashiwagi K., Suzuki T., Suzuki F., Furuchi T., Kobayashi H., Igarashi K.;
RT "Coexistence of the genes for putrescine transport protein and ornithine
RT decarboxylase at 16 min on Escherichia coli chromosome.";
RL J. Biol. Chem. 266:20922-20927(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
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 [4]
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 [5]
RP INDUCTION.
RC STRAIN=MRE-600;
RX PubMed=32094585; DOI=10.1038/s41564-020-0669-1;
RA Herrero Del Valle A., Seip B., Cervera-Marzal I., Sacheau G.,
RA Seefeldt A.C., Innis C.A.;
RT "Ornithine capture by a translating ribosome controls bacterial polyamine
RT synthesis.";
RL Nat. Microbiol. 5:554-561(2020).
CC -!- FUNCTION: The first enzyme leading to putrescine and thus polyamine
CC synthesis. {ECO:0000305}.
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:0000269|PubMed:1939141};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:1939141};
CC -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC L-ornithine pathway; putrescine from L-ornithine: step 1/1.
CC -!- INDUCTION: Induced at low environmental pH (at protein level). Part of
CC the speFL-speF-potE operon (PubMed:1939141). Expression induced by
CC ornithine (at protein level) (PubMed:32094585) (Probable).
CC {ECO:0000269|PubMed:1939141, ECO:0000269|PubMed:32094585,
CC ECO:0000305|PubMed:32094585}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC {ECO:0000305}.
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DR EMBL; M64495; AAA62785.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73787.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35349.1; -; Genomic_DNA.
DR PIR; A40839; A40839.
DR RefSeq; NP_415220.1; NC_000913.3.
DR RefSeq; WP_000040195.1; NZ_LN832404.1.
DR AlphaFoldDB; P24169; -.
DR SMR; P24169; -.
DR BioGRID; 4261018; 16.
DR DIP; DIP-154N; -.
DR IntAct; P24169; 4.
DR STRING; 511145.b0693; -.
DR PaxDb; P24169; -.
DR PRIDE; P24169; -.
DR EnsemblBacteria; AAC73787; AAC73787; b0693.
DR EnsemblBacteria; BAA35349; BAA35349; BAA35349.
DR GeneID; 945297; -.
DR KEGG; ecj:JW0680; -.
DR KEGG; eco:b0693; -.
DR PATRIC; fig|1411691.4.peg.1583; -.
DR EchoBASE; EB0957; -.
DR eggNOG; COG1982; Bacteria.
DR HOGENOM; CLU_014292_3_0_6; -.
DR InParanoid; P24169; -.
DR OMA; HIKGQPR; -.
DR PhylomeDB; P24169; -.
DR BioCyc; EcoCyc:ORNDECARBOXDEG-MON; -.
DR BioCyc; MetaCyc:ORNDECARBOXDEG-MON; -.
DR UniPathway; UPA00535; UER00288.
DR PRO; PR:P24169; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR GO; GO:0004586; F:ornithine decarboxylase activity; IDA:EcoCyc.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
DR GO; GO:0071468; P:cellular response to acidic pH; IEP:EcoCyc.
DR GO; GO:0033387; P:putrescine biosynthetic process from ornithine; IEA:UniProtKB-UniPathway.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
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; 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 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 TIGRFAMs; TIGR04301; ODC_inducible; 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..732
FT /note="Inducible ornithine decarboxylase"
FT /id="PRO_0000201135"
FT MOD_RES 355
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 732 AA; 82416 MW; C2C030BEAB9D23F6 CRC64;
MSKLKIAVSD SCPDCFTTQR ECIYINESRN IDVAAIVLSL NDVTCGKLDE IDATGYGIPV
FIATENQERV PAEYLPRISG VFENCESRRE FYGRQLETAA SHYETQLRPP FFRALVDYVN
QGNSAFDCPG HQGGEFFRRH PAGNQFVEYF GEALFRADLC NADVAMGDLL IHEGAPCIAQ
QHAAKVFNAD KTYFVLNGTS SSNKVVLNAL LTPGDLVLFD RNNHKSNHHG ALLQAGATPV
YLETARNPYG FIGGIDAHCF EESYLRELIA EVAPQRAKEA RPFRLAVIQL GTYDGTIYNA
RQVVDKIGHL CDYILFDSAW VGYEQFIPMM ADCSPLLLDL NENDPGILVT QSVHKQQAGF
SQTSQIHKKD SHIKGQQRYV PHKRMNNAFM MHASTSPFYP LFAALNINAK MHEGVSGRNM
WMDCVVNGIN ARKLILDNCQ HIRPFVPELV DGKPWQSYET AQIAVDLRFF QFVPGEHWHS
FEGYAENQYF VDPCKLLLTT PGIDARNGEY EAFGVPATIL ANFLRENGVV PEKCDLNSIL
FLLTPAEDMA KLQQLVALLV RFEKLLESDA PLAEVLPSIY KQHEERYAGY TLRQLCQEMH
DLYARHNVKQ LQKEMFRKEH FPRVSMNPQE ANYAYLRGEV ELVRLPDAEG RIAAEGALPY
PPGVLCVVPG EIWGGAVLRY FSALEEGINL LPGFAPELQG VYIEEHDGRK QVWCYVIKPR
DAQSTLLKGE KL
