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Database: UniProt
Entry: B1KVJ3_CLOBM
LinkDB: B1KVJ3_CLOBM
Original site: B1KVJ3_CLOBM 
ID   B1KVJ3_CLOBM            Unreviewed;       317 AA.
AC   B1KVJ3;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   SubName: Full=N(5)-(Carboxyethyl)ornithine synthase {ECO:0000313|EMBL:ACA55266.1};
DE            EC=1.5.1.24 {ECO:0000313|EMBL:ACA55266.1};
GN   Name=ceo {ECO:0000313|EMBL:ACA55266.1};
GN   OrderedLocusNames=CLK_3726 {ECO:0000313|EMBL:ACA55266.1};
OS   Clostridium botulinum (strain Loch Maree / Type A3).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498214 {ECO:0000313|EMBL:ACA55266.1, ECO:0000313|Proteomes:UP000000722};
RN   [1] {ECO:0000313|EMBL:ACA55266.1, ECO:0000313|Proteomes:UP000000722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Loch Maree / Type A3 {ECO:0000313|Proteomes:UP000000722};
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).
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DR   EMBL; CP000962; ACA55266.1; -; Genomic_DNA.
DR   RefSeq; WP_012343270.1; NC_010520.1.
DR   AlphaFoldDB; B1KVJ3; -.
DR   KEGG; cbl:CLK_3726; -.
DR   HOGENOM; CLU_055768_0_0_9; -.
DR   OMA; NEMAGYC; -.
DR   Proteomes; UP000000722; Chromosome.
DR   GO; GO:0047126; F:N5-(carboxyethyl)ornithine synthase activity; ISS:UniProtKB.
DR   CDD; cd12181; ceo_syn; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR007886; AlaDH/PNT_N.
DR   InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR   InterPro; IPR046951; CEOS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42795; ALANINE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42795:SF1; ALANINE DEHYDROGENASE; 1.
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; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ACA55266.1}.
FT   DOMAIN          4..111
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          147..273
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
SQ   SEQUENCE   317 AA;  35823 MW;  5F4FA3246846362A CRC64;
     MKLGFLIPNH PNEKRVALLP EHVKGFNNEL IVETGFGETL GISDAEYVKV GCTIASREEI
     FKTCEGVFSL KVLKPQDYKH IREGQIIVGW THPEGSGKTF MEEQGIPKNL IIVDLDNIHP
     SIYYKDYVIP MEWIPSNFVR KNSYIAGYAS TMHAVMNYGS IPTSETKVAI LGSGNVSQGA
     FSAISKFNPD IRMFYRKTMN QLKDELEEFD IIINGIEMDN PNKHILTLED QMRLKKNCLI
     IDAAANLGKA IEGARHTTAS DPIYNKDGKY YYAVNNSPSI FYRQSSKAIS EAFSKHVYSK
     ELEFYLDVIA EVEEMIV
//
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