Reviewed, UniProtKB/Swiss-Prot P15244 (CEO2_LACLA)

Names and origin

Protein names

Recommended name:
    N(5)-(carboxyethyl)ornithine synthase
    EC=1.5.1.24
Alternative name(s):
    N(5)-(L-1-carboxyethyl)-L-ornithine:NADP(+) oxidoreductase
      Short name=CEOS

Gene names

Name:

ceo

Organism

Lactococcus lactis subsp. lactis (Streptococcus lactis)

Taxonomic identifier

1360 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Lactococcus

Protein attributes

Sequence length	313 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	N(5)-(L-1-carboxyethyl)-L-ornithine + NADP+ + H2O = L-ornithine + pyruvate + NADPH.
Subunit structure	Homotetramer.
Miscellaneous	In the reverse direction L-lysine can act instead of L-ornithine, more slowly, yielding N(6)-(L-1-carboxyethyl)-L-lysine.
Mass spectrometry	Molecular mass is 35355 Da from positions 1 - 313. Determined by MALDI. Ref.3

Ontologies

Keywords
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	N5-(carboxyethyl)ornithine synthase activity Inferred from electronic annotation. Source: EC binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 313	313	N(5)-(carboxyethyl)ornithine synthase		PRO_0000089483
Regions
	Nucleotide binding	171 – 176	6	NADP Potential
Experimental info
	Mutagenesis	15	1	R → K: Loss of activity. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P15244-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: B17FE0F477113C77	FASTA	313	35,323
	10 20 30 40 50 60 MKIGLVKANF PGERRVPLLP KDIKDFKNEI LVEEGFGKFL DIDDQEYSDK GCHILSRAEV 70 80 90 100 110 120 FAESEAIFSL KLIQPTDYYH LREGQMIIGW THPFGSGQSF MKEQALPKKL IVVDLDSNSP 130 140 150 160 170 180 CIYYENEIFE SGIPKGLLYK NSFYAGYAGV LDALLQYGLI PTEETKIAIL GSGNVAQGAF 190 200 210 220 230 240 SSISKYSSNI RMYYRKTMSI FKENYTKYDI IINGIEIGKD DDPILSFSEQ KSLKKGTLII 250 260 270 280 290 300 DVAADAGNTI EGSHFTSIDA PIYENAGKYY YVVPNTPSLI YRNVSQELSK ILSENIFRKD 310 CSRFIEKVKP LNK

References

[1]	"Cloning, expression, sequence analysis, and site-directed mutagenesis of the Tn5306-encoded N(5)-(carboxyethyl)ornithine synthase from Lactococcus lactis K1." Donkersloot J.A., Thompson J. J. Biol. Chem. 270:12226-12234(1995) [PubMed: 7744873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF ARG-15. Strain: K1-23. Transposon: Tn5306.
[2]	"N(5)-(L-1-carboxyethyl)-L-ornithine:NADP(+) oxidoreductase from Streptococcus lactis. Purification and partial characterization." Thompson J. J. Biol. Chem. 264:9592-9601(1989) [PubMed: 2498334] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-37. Strain: K1.
[3]	"N(5)-(L-1-carboxyethyl)-L-ornithine synthase: physical and spectral characterization of the enzyme and its unusual low pKa fluorescent tyrosine residues." Sackett D.L., Ruvinov S.B., Thompson J. Protein Sci. 8:2121-2129(1999) [PubMed: 10548058] [Abstract] Cited for: PROTEIN SEQUENCE OF 256-263, CHARACTERIZATION, MASS SPECTROMETRY. Strain: K1.
[4]	"Tetrameric N(5)-(L-1-carboxyethyl)-L-ornithine synthase: guanidine. HCl-induced unfolding and a low temperature requirement for refolding." Ruvinov S.B., Thompson J., Sackett D.L., Ginsburg A. Arch. Biochem. Biophys. 371:115-123(1999) [PubMed: 10525296] [Abstract] Cited for: FOLDING STUDIES. Strain: K1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U23376 Genomic DNA. Translation: AAA86385.1.
PIR	A57499.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.5.1.24. 278870.
Family and domain databases
InterPro	IPR007698. Ala_DH/PNT_C. IPR007886. Ala_DH/PNT_N. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF01262. AlaDh_PNT_C. 1 hit. PF05222. AlaDh_PNT_N. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CEO2_LACLA

Accession

Primary (citable) accession number: P15244

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 60 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)