LDCC_ECOLI
ID LDCC_ECOLI Reviewed; 713 AA.
AC P52095; P78299;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Constitutive lysine decarboxylase;
DE Short=LDCC;
DE EC=4.1.1.18 {ECO:0000269|PubMed:9339543};
GN Name=ldcC; Synonyms=ldc, ldcH; OrderedLocusNames=b0186, JW0181;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP CHARACTERIZATION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9226257; DOI=10.1128/jb.179.14.4486-4492.1997;
RA Kikuchi Y., Kojima H., Tanaka T., Takatsuka Y., Kamio Y.;
RT "Characterization of a second lysine decarboxylase isolated from
RT Escherichia coli.";
RL J. Bacteriol. 179:4486-4492(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-40 AND 415-456,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9339543; DOI=10.1266/ggs.72.167;
RA Yamamoto Y., Miwa Y., Miyoshi K., Furuyama J., Ohmori H.;
RT "The Escherichia coli ldcC gene encodes another lysine decarboxylase,
RT probably a constitutive enzyme.";
RL Genes Genet. Syst. 72:167-172(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 555-713.
RC STRAIN=K12;
RX PubMed=9723924; DOI=10.1046/j.1365-2958.1998.00981.x;
RA Pichoff S., Alibaud L., Guedant A., Castanie M.-P., Bouche J.-P.;
RT "An Escherichia coli gene (yaeO) suppresses temperature-sensitive mutations
RT in essential genes by modulating Rho-dependent transcription termination.";
RL Mol. Microbiol. 29:859-869(1998).
RN [8]
RP INDUCTION BY RPOS.
RX PubMed=9692215; DOI=10.1271/bbb.62.1267;
RA Kikuchi Y., Kurahashi O., Nagano T., Kamio Y.;
RT "RpoS-dependent expression of the second lysine decarboxylase gene in
RT Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 62:1267-1270(1998).
RN [9]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.50 ANGSTROMS) OF 1-710, AND SUBUNIT.
RX PubMed=27080013; DOI=10.1038/srep24601;
RA Kandiah E., Carriel D., Perard J., Malet H., Bacia M., Liu K., Chan S.W.,
RA Houry W.A., Ollagnier de Choudens S., Elsen S., Gutsche I.;
RT "Structural insights into the Escherichia coli lysine decarboxylases and
RT molecular determinants of interaction with the AAA+ ATPase RavA.";
RL Sci. Rep. 6:24601-24601(2016).
CC -!- FUNCTION: Plays a role in lysine utilization by acting as a lysine
CC decarboxylase. {ECO:0000269|PubMed:9339543}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-lysine = cadaverine + CO2; Xref=Rhea:RHEA:22352,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32551,
CC ChEBI:CHEBI:58384; EC=4.1.1.18;
CC Evidence={ECO:0000269|PubMed:9339543};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.2-8.0.;
CC -!- SUBUNIT: Homodecamer; built of five dimers associated in a 5-fold
CC symmetrical double-ring. {ECO:0000269|PubMed:27080013}.
CC -!- INTERACTION:
CC P52095; P0A9H3: cadA; NbExp=5; IntAct=EBI-545944, EBI-545922;
CC -!- INDUCTION: By RpoS-dependent mechanism on stationary phase on the
CC contrary to the second lysine decarboxylase CadA which is not induced
CC by RpoS. {ECO:0000269|PubMed:9692215}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D87518; BAA21656.1; -; Genomic_DNA.
DR EMBL; D49445; BAA08426.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08615.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73297.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77861.1; -; Genomic_DNA.
DR EMBL; Z50870; CAA90749.1; -; Genomic_DNA.
DR PIR; B64743; B64743.
DR RefSeq; NP_414728.1; NC_000913.3.
DR RefSeq; WP_001020973.1; NZ_STEB01000032.1.
DR PDB; 5FKZ; EM; 5.50 A; E=1-710.
DR PDBsum; 5FKZ; -.
DR AlphaFoldDB; P52095; -.
DR SMR; P52095; -.
DR BioGRID; 4259757; 9.
DR DIP; DIP-10086N; -.
DR IntAct; P52095; 5.
DR STRING; 511145.b0186; -.
DR jPOST; P52095; -.
DR PaxDb; P52095; -.
DR PRIDE; P52095; -.
DR EnsemblBacteria; AAC73297; AAC73297; b0186.
DR EnsemblBacteria; BAA77861; BAA77861; BAA77861.
DR GeneID; 66671526; -.
DR GeneID; 944887; -.
DR KEGG; ecj:JW0181; -.
DR KEGG; eco:b0186; -.
DR PATRIC; fig|1411691.4.peg.2093; -.
DR EchoBASE; EB3010; -.
DR eggNOG; COG1982; Bacteria.
DR InParanoid; P52095; -.
DR OMA; WSTLLTE; -.
DR PhylomeDB; P52095; -.
DR BioCyc; EcoCyc:LDC2-MON; -.
DR BioCyc; MetaCyc:LDC2-MON; -.
DR BRENDA; 4.1.1.18; 2026.
DR PRO; PR:P52095; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0008923; F:lysine decarboxylase activity; IDA:EcoCyc.
DR GO; GO:0006554; P:lysine catabolic process; IDA:EcoliWiki.
DR CDD; cd00615; Orn_deC_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
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; 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; SSF53383; SSF53383; 1.
DR SUPFAM; SSF55904; SSF55904; 1.
DR PROSITE; PS00703; OKR_DC_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Direct protein sequencing; Lyase;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..713
FT /note="Constitutive lysine decarboxylase"
FT /id="PRO_0000201142"
FT MOD_RES 367
FT /note="N6-(pyridoxal phosphate)lysine"
FT CONFLICT 284
FT /note="S -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="N -> F (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="T -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 413..414
FT /note="AA -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="M -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 673
FT /note="L -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 713 AA; 80590 MW; 4532C6069744ABDF CRC64;
MNIIAIMGPH GVFYKDEPIK ELESALVAQG FQIIWPQNSV DLLKFIEHNP RICGVIFDWD
EYSLDLCSDI NQLNEYLPLY AFINTHSTMD VSVQDMRMAL WFFEYALGQA EDIAIRMRQY
TDEYLDNITP PFTKALFTYV KERKYTFCTP GHMGGTAYQK SPVGCLFYDF FGGNTLKADV
SISVTELGSL LDHTGPHLEA EEYIARTFGA EQSYIVTNGT STSNKIVGMY AAPSGSTLLI
DRNCHKSLAH LLMMNDVVPV WLKPTRNALG ILGGIPRREF TRDSIEEKVA ATTQAQWPVH
AVITNSTYDG LLYNTDWIKQ TLDVPSIHFD SAWVPYTHFH PIYQGKSGMS GERVAGKVIF
ETQSTHKMLA ALSQASLIHI KGEYDEEAFN EAFMMHTTTS PSYPIVASVE TAAAMLRGNP
GKRLINRSVE RALHFRKEVQ RLREESDGWF FDIWQPPQVD EAECWPVAPG EQWHGFNDAD
ADHMFLDPVK VTILTPGMDE QGNMSEEGIP AALVAKFLDE RGIVVEKTGP YNLLFLFSIG
IDKTKAMGLL RGLTEFKRSY DLNLRIKNML PDLYAEDPDF YRNMRIQDLA QGIHKLIRKH
DLPGLMLRAF DTLPEMIMTP HQAWQRQIKG EVETIALEQL VGRVSANMIL PYPPGVPLLM
PGEMLTKESR TVLDFLLMLC SVGQHYPGFE TDIHGAKQDE DGVYRVRVLK MAG
