CEO_CLOBH
ID CEO_CLOBH Reviewed; 317 AA.
AC A5HZ59; A7FZS5;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=CBO0515, CLC_0588;
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX PubMed=17519437; DOI=10.1101/gr.6282807;
RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA White B., Whithead S., Parkhill J.;
RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT Hall A and comparative analysis of the clostridial genomes.";
RL Genome Res. 17:1082-1092(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
RN [3]
RP PROTEIN SEQUENCE OF 1-28, FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS,
RP SUBSTRATE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT,
RP MUTAGENESIS OF GLU-13; ARG-15; LYS-71; TRP-90; HIS-92 AND ASP-114, AND
RP PYRUVATE BINDING SITE.
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX PubMed=19933367; DOI=10.1128/jb.01044-09;
RA Thompson J., Hill K.K., Smith T.J., Pikis A.;
RT "The gene CBO0515 from Clostridium botulinum strain Hall A encodes the rare
RT enzyme N5-(carboxyethyl) ornithine synthase, EC 1.5.1.24.";
RL J. Bacteriol. 192:1151-1155(2010).
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), and
CC the D-isomers of the 2 basic amino acids. Can use alpha-keto acids
CC other than pyruvate, e.g. glyoxylate. {ECO:0000269|PubMed:19933367}.
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 Evidence={ECO:0000269|PubMed:19933367};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.15 mM for pyruvate {ECO:0000269|PubMed:19933367};
CC KM=29.5 mM for L-ornithine {ECO:0000269|PubMed:19933367};
CC KM=2.95 uM for NADPH {ECO:0000269|PubMed:19933367};
CC Vmax=22.4 umol/min/mg enzyme {ECO:0000269|PubMed:19933367};
CC -!- SUBUNIT: Homotetramer. {ECO:0000305|PubMed:19933367}.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family. CEOS subfamily.
CC {ECO:0000305}.
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DR EMBL; CP000727; ABS38175.1; -; Genomic_DNA.
DR EMBL; AM412317; CAL82068.1; -; Genomic_DNA.
DR RefSeq; WP_011948261.1; NC_009698.1.
DR RefSeq; YP_001253058.1; NC_009495.1.
DR RefSeq; YP_001386471.1; NC_009698.1.
DR AlphaFoldDB; A5HZ59; -.
DR SMR; A5HZ59; -.
DR GeneID; 5184770; -.
DR KEGG; cbh:CLC_0588; -.
DR KEGG; cbo:CBO0515; -.
DR PATRIC; fig|413999.7.peg.517; -.
DR HOGENOM; CLU_055768_0_0_9; -.
DR OMA; NEMAGYC; -.
DR SABIO-RK; A5HZ59; -.
DR PRO; PR:A5HZ59; -.
DR Proteomes; UP000001986; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0047126; F:N5-(carboxyethyl)ornithine synthase activity; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IBA:GO_Central.
DR GO; GO:0008746; F:NAD(P)+ transhydrogenase activity; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IBA:GO_Central.
DR GO; GO:0006740; P:NADPH regeneration; IBA:GO_Central.
DR GO; GO:0006591; P:ornithine metabolic process; IDA: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 1: Evidence at protein level;
KW Direct protein sequencing; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..317
FT /note="N(5)-(carboxyethyl)ornithine synthase"
FT /id="PRO_0000393238"
FT BINDING 15
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000305"
FT BINDING 71
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000305"
FT BINDING 92
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000305"
FT BINDING 172..177
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT MUTAGEN 13
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19933367"
FT MUTAGEN 15
FT /note="R->K: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19933367"
FT MUTAGEN 71
FT /note="K->R: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19933367"
FT MUTAGEN 90
FT /note="W->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19933367"
FT MUTAGEN 92
FT /note="H->L: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19933367"
FT MUTAGEN 114
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19933367"
SQ SEQUENCE 317 AA; 35849 MW; 79F3FCA31C50C4F3 CRC64;
MKLGFLIPNH PNEKRVALLP EHVKGFNNEL VIETGFGETL GISDAEYVKV GCTIASREEI
FKTCEGIFSL KVLKPQDYKH IREGQIIVGW THPEGSGKIF MEEQGIPKNL IIVDLDNIHP
SIYYKDYVIP MEWIPSNFVR KNSYIAGYAS TMHAVMNYGS IPTSETKVAI LGSGNVSQGA
FSAISKFNPD IRMFYRKTMN QLKDELEEFD IIINGIEMDN PNKHILTLED QMRLKKNCLI
IDAAANLGKA IEGARHTTAS DPIYNKDGKY YYAVNNSPSI FYRQSSKAIS EAFSKHVYSK
ELEFYLDVIA EVEEMIV
