ID   CEO1_LACLA              Reviewed;         309 AA.
AC   Q9CG73;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=N(5)-(carboxyethyl)ornithine synthase;
DE            Short=CEOS;
DE            EC=1.5.1.24;
DE   AltName: Full=N(5)-(L-1-carboxyethyl)-L-ornithine:NADP(+) oxidoreductase;
GN   Name=ceo; OrderedLocusNames=LL1237; ORFNames=L64332;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reductive condensation between
CC       pyruvic acid and the side chain amino group of L-ornithine to form
CC       N(5)-(L-1-carboxyethyl)-L-ornithine. To a lesser extent, can also use
CC       L-lysine as substrate (yielding N(6)-(L-1-carboxyethyl)-L-lysine) (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(5)-[1(S)-1-carboxyethyl]-L-ornithine + NADP(+) = H(+)
CC         + L-ornithine + NADPH + pyruvate; Xref=Rhea:RHEA:18661,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:46911, ChEBI:CHEBI:57783, ChEBI:CHEBI:57889,
CC         ChEBI:CHEBI:58349; EC=1.5.1.24;
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AlaDH/PNT family. CEOS subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE005176; AAK05335.1; -; Genomic_DNA.
DR   PIR; E86779; E86779.
DR   RefSeq; NP_267393.1; NC_002662.1.
DR   RefSeq; WP_003131029.1; NC_002662.1.
DR   AlphaFoldDB; Q9CG73; -.
DR   SMR; Q9CG73; -.
DR   STRING; 272623.L64332; -.
DR   PaxDb; Q9CG73; -.
DR   EnsemblBacteria; AAK05335; AAK05335; L64332.
DR   KEGG; lla:L64332; -.
DR   PATRIC; fig|272623.7.peg.1338; -.
DR   eggNOG; COG0686; Bacteria.
DR   HOGENOM; CLU_055768_0_0_9; -.
DR   OMA; NEMAGYC; -.
DR   Proteomes; UP000002196; Chromosome.
DR   GO; GO:0047126; F:N5-(carboxyethyl)ornithine synthase activity; ISS:UniProtKB.
DR   InterPro; IPR007886; AlaDH/PNT_N.
DR   InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01262; AlaDh_PNT_C; 1.
DR   Pfam; PF05222; AlaDh_PNT_N; 1.
DR   SMART; SM01002; AlaDh_PNT_C; 1.
DR   SMART; SM01003; AlaDh_PNT_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..309
FT                   /note="N(5)-(carboxyethyl)ornithine synthase"
FT                   /id="PRO_0000089482"
FT   BINDING         15
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000250"
FT   BINDING         71
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000250"
FT   BINDING         171..176
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   309 AA;  35008 MW;  51C5E5ED8DE508FA CRC64;
     MKIGLVKTNF PGERRVPLLP KDIKDFKNEI LVEEGFGKFL DIDDQEYIDK GCHILSRAEV
     FSESEAIFSL KLIQPTDYPY LREGQMIIGW THPFGSGRLF MKEQALPKKL IVVDLDSNSP
     CIYYENEIFE SGIPKGLLYK NSFYAGYAGV LDALLQYGFI PTEETKIAIL GSGNVAQGAF
     SSISKYSSNI RMYYRKTMSI FKENYTKYDI IINGIEIGKE DDPILSFSEQ KSLKKGTFII
     DVAADAGNTI EGTHFTSMDD PIYENDGKYY YVVPNTPSLI YRNVSQDLSK ILSENIFSED
     CSRFLSIKS