ID   CEO2_LACLA              Reviewed;         313 AA.
AC   P15244;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   04-NOV-2008, entry version 56.
DE   RecName: Full=N(5)-(carboxyethyl)ornithine synthase;
DE            EC=1.5.1.24;
DE   AltName: Full=N(5)-(L-1-carboxyethyl)-L-ornithine:NADP(+) oxidoreductase;
DE            Short=CEOS;
GN   Name=ceo;
OS   Lactococcus lactis subsp. lactis (Streptococcus lactis).
OC   Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; Lactococcus.
OX   NCBI_TaxID=1360;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF ARG-15.
RC   STRAIN=K1-23; TRANSPOSON=Tn5306;
RX   MEDLINE=95263576; PubMed=7744873; DOI=10.1074/jbc.270.20.12226;
RA   Donkersloot J.A., Thompson J.;
RT   "Cloning, expression, sequence analysis, and site-directed mutagenesis
RT   of the Tn5306-encoded N(5)-(carboxyethyl)ornithine synthase from
RT   Lactococcus lactis K1.";
RL   J. Biol. Chem. 270:12226-12234(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-37.
RC   STRAIN=K1;
RX   MEDLINE=89255467; PubMed=2498334;
RA   Thompson J.;
RT   "N(5)-(L-1-carboxyethyl)-L-ornithine:NADP(+) oxidoreductase from
RT   Streptococcus lactis. Purification and partial characterization.";
RL   J. Biol. Chem. 264:9592-9601(1989).
RN   [3]
RP   PROTEIN SEQUENCE OF 256-263, CHARACTERIZATION, AND MASS SPECTROMETRY.
RC   STRAIN=K1;
RX   MEDLINE=20014035; PubMed=10548058;
RA   Sackett D.L., Ruvinov S.B., Thompson J.;
RT   "N(5)-(L-1-carboxyethyl)-L-ornithine synthase: physical and spectral
RT   characterization of the enzyme and its unusual low pKa fluorescent
RT   tyrosine residues.";
RL   Protein Sci. 8:2121-2129(1999).
RN   [4]
RP   FOLDING STUDIES.
RC   STRAIN=K1;
RX   MEDLINE=99456521; PubMed=10525296; DOI=10.1006/abbi.1999.1429;
RA   Ruvinov S.B., Thompson J., Sackett D.L., Ginsburg A.;
RT   "Tetrameric N(5)-(L-1-carboxyethyl)-L-ornithine synthase: guanidine.
RT   HCl-induced unfolding and a low temperature requirement for
RT   refolding.";
RL   Arch. Biochem. Biophys. 371:115-123(1999).
CC   -!- CATALYTIC ACTIVITY: N(5)-(L-1-carboxyethyl)-L-ornithine + NADP(+)
CC       + H(2)O = L-ornithine + pyruvate + NADPH.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- MASS SPECTROMETRY: Mass=35355; Method=MALDI; Range=1-313;
CC       Source=PubMed:10548058;
CC   -!- MISCELLANEOUS: In the reverse direction L-lysine can act instead
CC       of L-ornithine, more slowly, yielding N(6)-(L-1-carboxyethyl)-L-
CC       lysine.
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DR   EMBL; U23376; AAA86385.1; -; Genomic_DNA.
DR   PIR; A57499; A57499.
DR   GO; GO:0047126; F:N5-(carboxyethyl)ornithine synthase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR007698; Ala_DHase/PNT_C.
DR   InterPro; IPR007886; Ala_DHase/PNT_N.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF01262; AlaDh_PNT_C; 1.
DR   Pfam; PF05222; AlaDh_PNT_N; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NADP; Oxidoreductase.
FT   CHAIN         1    313       N(5)-(carboxyethyl)ornithine synthase.
FT                                /FTId=PRO_0000089483.
FT   NP_BIND     171    176       NADP (Potential).
FT   MUTAGEN      15     15       R->K: Loss of activity.
SQ   SEQUENCE   313 AA;  35323 MW;  B17FE0F477113C77 CRC64;
     MKIGLVKANF PGERRVPLLP KDIKDFKNEI LVEEGFGKFL DIDDQEYSDK GCHILSRAEV
     FAESEAIFSL KLIQPTDYYH LREGQMIIGW THPFGSGQSF MKEQALPKKL IVVDLDSNSP
     CIYYENEIFE SGIPKGLLYK NSFYAGYAGV LDALLQYGLI PTEETKIAIL GSGNVAQGAF
     SSISKYSSNI RMYYRKTMSI FKENYTKYDI IINGIEIGKD DDPILSFSEQ KSLKKGTLII
     DVAADAGNTI EGSHFTSIDA PIYENAGKYY YVVPNTPSLI YRNVSQELSK ILSENIFRKD
     CSRFIEKVKP LNK
//