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Database: UniProt
Entry: C5BC25_EDWI9
LinkDB: C5BC25_EDWI9
Original site: C5BC25_EDWI9 
ID   C5BC25_EDWI9            Unreviewed;       812 AA.
AC   C5BC25;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   03-JUL-2019, entry version 65.
DE   RecName: Full=Bifunctional aspartokinase/homoserine dehydrogenase {ECO:0000256|PIRNR:PIRNR000727};
DE   Includes:
DE     RecName: Full=Aspartokinase {ECO:0000256|PIRNR:PIRNR000727};
DE              EC=2.7.2.4 {ECO:0000256|PIRNR:PIRNR000727};
DE   Includes:
DE     RecName: Full=Homoserine dehydrogenase {ECO:0000256|PIRNR:PIRNR000727};
DE              EC=1.1.1.3 {ECO:0000256|PIRNR:PIRNR000727};
GN   OrderedLocusNames=NT01EI_3806 {ECO:0000313|EMBL:ACR70931.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR70931.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACR70931.1, ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|EMBL:ACR70931.1,
RC   ECO:0000313|Proteomes:UP000001485};
RX   PubMed=22247535; DOI=10.1128/JB.06522-11;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Banes M.M.,
RA   Lawrence M.L.;
RT   "Genome Sequence of Edwardsiella ictaluri 93-146, a Strain Associated
RT   with a Natural Channel Catfish Outbreak of Enteric Septicemia of
RT   Catfish.";
RL   J. Bacteriol. 194:740-741(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-aspartate = 4-phospho-L-aspartate + ADP;
CC         Xref=Rhea:RHEA:23776, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57535, ChEBI:CHEBI:456216; EC=2.7.2.4;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000727};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4-
CC         semialdehyde + NADPH; Xref=Rhea:RHEA:15761, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57476, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:537519; EC=1.1.1.3;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000727};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
CC       {ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-homoserine from L-aspartate: step 1/3.
CC       {ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-homoserine from L-aspartate: step 3/3.
CC       {ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 1/5.
CC       {ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 3/5.
CC       {ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the homoserine
CC       dehydrogenase family. {ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       aspartokinase family. {ECO:0000256|PIRNR:PIRNR000727}.
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DR   EMBL; CP001600; ACR70931.1; -; Genomic_DNA.
DR   RefSeq; WP_015872964.1; NC_012779.2.
DR   EnsemblBacteria; ACR70931; ACR70931; NT01EI_3806.
DR   GeneID; 7959853; -.
DR   KEGG; eic:NT01EI_3806; -.
DR   PATRIC; fig|634503.3.peg.3400; -.
DR   eggNOG; ENOG4105CFH; Bacteria.
DR   eggNOG; COG0460; LUCA.
DR   eggNOG; COG0527; LUCA.
DR   HOGENOM; HOG000271594; -.
DR   KO; K12525; -.
DR   OMA; GAGVCKN; -.
DR   OrthoDB; 1067792at2; -.
DR   BioCyc; EICT634503:G1GVC-3478-MONOMER; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04257; AAK_AK-HSDH; 1.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR041743; AK-HSDH_N.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR   InterPro; IPR018042; Aspartate_kinase_CS.
DR   InterPro; IPR011147; Bifunc_aspartokin/hSer_DH.
DR   InterPro; IPR001342; HDH_cat.
DR   InterPro; IPR019811; HDH_CS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF00742; Homoserine_dh; 1.
DR   Pfam; PF03447; NAD_binding_3; 1.
DR   PIRSF; PIRSF000727; ThrA; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   PROSITE; PS00324; ASPARTOKINASE; 1.
DR   PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR000727};
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR000727};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000727, ECO:0000313|EMBL:ACR70931.1};
KW   NADP {ECO:0000256|PIRNR:PIRNR000727};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000727};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000727,
KW   ECO:0000313|EMBL:ACR70931.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000727,
KW   ECO:0000313|EMBL:ACR70931.1}.
FT   DOMAIN       14    286       AA_kinase. {ECO:0000259|Pfam:PF00696}.
FT   DOMAIN      467    602       NAD_binding_3. {ECO:0000259|Pfam:
FT                                PF03447}.
FT   DOMAIN      610    805       Homoserine_dh. {ECO:0000259|Pfam:
FT                                PF00742}.
SQ   SEQUENCE   812 AA;  89212 MW;  5858141C886E656B CRC64;
     MSAQAVTGQQ QADRQLHKFG GSSLADVKCY LRVAGIMAEY SRPGDMMVVS AAGSTTNQLI
     SWLKLSQSDR ISAHQVQQAL RRYQSELIVG LLPPEMAEPL QTHFIRDLER LAALLDGEMD
     EAAYAEVVGH GEVWSARLMA AVLQSQGLEA TWLDARDFLC AEHAAQPQVD ERRSYPLLQQ
     LLAQHPNKRL VVTGFISRSG AGETVLLGRN GSDYSATQIG ALAGVRRVTI WSDVAGVYSA
     DPRKVKDACL LPLLRLDEAS ELARLAAPVL HARTLQPVSA SDIDLQLRCS YQPQQGSTRI
     ERVLASGNGA KIVTSHDDVC LIELHVTTGH EFSHIHQEVE RILTRSQLRP LASGIHRDRG
     LIQLCYTAEV VGSVFKLLEE SAIPGLLQLR EGLALVAMVG AGVCRNPLHA HRFYQQLKDQ
     PVEFIWQSEE SISLVAVLRC GPTEALVQGL HNSLFRAEKR VGLVLFGKGN IGSRWLELFA
     REQGNLSASS GFEFILTGVV DSNRSLLNYD GLDASRALAF FDDEAQVLDE ESLFLWMRAH
     PYDDLVVLDV TASPSLAQQY RDFASYGFHM VSANKLAGAA GGHEYRQIRD AFEKTGRHWL
     YNATVGAGLP VNYTVRDLRD SGDTILSISG IFSGTLSWLF LQFDGSIPFS ALVDQAWQQG
     LTEPDPRVDL SGQDVMRKLV ILAREAGYDI EPAQVRVESL VPAGGEQGSI DHFFENSEAL
     DEQMLQRLAA ANEMGLVLRY VARFDANGKA RVGVEAVRPE HPLASLLPCD NVFAIESRWY
     RDNPLVIRGP GAGRDVTAGA IQSDLNRLAR LL
//
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