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Database: UniProt
Entry: A0A0J8VRL3_9ENTR
LinkDB: A0A0J8VRL3_9ENTR
Original site: A0A0J8VRL3_9ENTR 
ID   A0A0J8VRL3_9ENTR        Unreviewed;       810 AA.
AC   A0A0J8VRL3;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   08-MAY-2019, entry version 22.
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   Name=metL {ECO:0000313|EMBL:KMV35567.1};
GN   ORFNames=ACH50_06595 {ECO:0000313|EMBL:KMV35567.1};
OS   Franconibacter pulveris.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Franconibacter.
OX   NCBI_TaxID=435910 {ECO:0000313|EMBL:KMV35567.1, ECO:0000313|Proteomes:UP000037315};
RN   [1] {ECO:0000313|EMBL:KMV35567.1, ECO:0000313|Proteomes:UP000037315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ34 {ECO:0000313|EMBL:KMV35567.1,
RC   ECO:0000313|Proteomes:UP000037315};
RA   Pal S., Banerjee T.D., Roy A., Sar P., Kazy S.K.;
RT   "Genome sequencing of Cronobacter sp. strain DJ34 isolated from
RT   petroleum contaminated sludge of Duliajan Oil Fields, Assam, India.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KMV35567.1}.
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DR   EMBL; LFEJ01000010; KMV35567.1; -; Genomic_DNA.
DR   RefSeq; WP_024556733.1; NZ_LFEJ01000010.1.
DR   EnsemblBacteria; KMV35567; KMV35567; ACH50_06595.
DR   PATRIC; fig|1656095.3.peg.624; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000037315; Unassembled WGS sequence.
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; IPR001341; Asp_kinase.
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   TIGRFAMs; TIGR00657; asp_kinases; 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:UP000037315};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000727, ECO:0000313|EMBL:KMV35567.1};
KW   NADP {ECO:0000256|PIRNR:PIRNR000727};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000727};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000727,
KW   ECO:0000313|EMBL:KMV35567.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037315};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000727,
KW   ECO:0000313|EMBL:KMV35567.1}.
FT   DOMAIN       12    284       AA_kinase. {ECO:0000259|Pfam:PF00696}.
FT   DOMAIN      465    600       NAD_binding_3. {ECO:0000259|Pfam:
FT                                PF03447}.
FT   DOMAIN      608    803       Homoserine_dh. {ECO:0000259|Pfam:
FT                                PF00742}.
SQ   SEQUENCE   810 AA;  88721 MW;  5E9B52CD4C6ECE64 CRC64;
     MSVTAPAGTK GRQLHKFGGS SLADVKCYLR VAGIMADYSL PGDMMVVSAA GSTTNQLISW
     LKLSQSDRLS AHQVQQALRR YQSELISGLL PPDVADGLIS EFIHDLERLA GLLDGTITDA
     VYAEVVGHGE VWSARLMAAV LNQQGLEAAW LDARDFLRAE RAAQPQVNEG LSYPLLQQLL
     VQHPGKRVVV TGFICRNDAG ETVLLGRNGS DYSATQIGAL AGVSRVTIWS DVAGVYSADP
     RKVKDACLLP LLRLDEASEL ARLAAPVLHA RTLQPVSGSD IDLQLRCSYN PEQGSTRIER
     VLASGTGARI VTSHDDVCLI EFEVASHQDF KLAHKEVDAL LKRAQVRPLS VGVHPDRSLL
     QLCYTSEVVG SALQILEEAG LPGELRLREG LALVALVGAG VCRNPLHSHR FWQQLKDQPV
     EFIWQSDDGI SLVAVLRVGP TEHLIQGLHQ SLFRAEKRIG LMLFGKGNIG SRWLELFARE
     QETFSARTGF EFVLAGVVDS RRSLLNYNGL DASRALAFFN DEAVEHDEES LFLWMRAHPY
     DDLVVLDVTA SQELADQYLD FASHGFHVIS ANKLAGASTS NKFRQIRDAF AKTGRHWLYN
     ATVGAGLPVN HTVRDLRDSG DNILAISGIF SGTLSWLFLQ FDGTVPFTDL VDQAWQQGLT
     EPDPRVDLSG KDVMRKLVIL AREAGYDIEP EQVRVESLVP AGCEAGSVDH FFENGDELNE
     QMVQRLEAAR EMGLVLRYVA RFDASGKARV GVEAVRAEHP LASLLPCDNV FAIESRWYRD
     NPLVIRGPGA GRDVTAGAIQ SDLNRLAQLL
//
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