ID   AKH_BUCAP               Reviewed;         814 AA.
AC   Q8K9U9;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-NOV-2008, entry version 46.
DE   RecName: Full=Bifunctional aspartokinase/homoserine dehydrogenase;
DE            Short=AK-HD;
DE   Includes:
DE     RecName: Full=Aspartokinase;
DE              EC=2.7.2.4;
DE   Includes:
DE     RecName: Full=Homoserine dehydrogenase;
DE              EC=1.1.1.3;
GN   Name=thrA; OrderedLocusNames=BUsg_188;
OS   Buchnera aphidicola subsp. Schizaphis graminum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=98794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
CC   -!- CATALYTIC ACTIVITY: L-homoserine + NAD(P)(+) = L-aspartate 4-
CC       semialdehyde + NAD(P)H.
CC   -!- CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L-
CC       aspartate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; tetrahydrodipicolinate from L-aspartate: step 1/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-homoserine from L-aspartate: step 1/3.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-homoserine from L-aspartate: step 3/3.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 1/5.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 3/5.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       aspartokinase family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the homoserine
CC       dehydrogenase family.
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DR   EMBL; AE013218; AAM67753.1; -; Genomic_DNA.
DR   RefSeq; NP_660542.1; -.
DR   HSSP; P31116; 1EBF.
DR   GeneID; 1005385; -.
DR   GenomeReviews; AE013218_GR; BUsg_188.
DR   KEGG; bas:BUsg188; -.
DR   HOGENOM; Q8K9U9; -.
DR   BioCyc; BAPH198804:BUSG188-MON; -.
DR   GO; GO:0004072; F:aspartate kinase activity; IEA:InterPro.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR005106; Asp/hSer_DHase_NAD-bd.
DR   InterPro; IPR001341; Asp_kin_reg.
DR   InterPro; IPR011147; bifunc_aspartokin/hSer_DHase.
DR   InterPro; IPR001342; hSer_DHase_cat.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   Gene3D; G3DSA:3.40.1160.10; Aa_kinase; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
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   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; Complete proteome; Kinase;
KW   Multifunctional enzyme; NADP; Oxidoreductase; Threonine biosynthesis;
KW   Transferase.
FT   CHAIN         1    814       Bifunctional aspartokinase/homoserine
FT                                dehydrogenase.
FT                                /FTId=PRO_0000066685.
FT   NP_BIND     470    477       NADP (Potential).
FT   REGION        1    248       Aspartokinase (By similarity).
FT   REGION      249    469       Interface (By similarity).
FT   REGION      470    814       Homoserine dehydrogenase (By similarity).
SQ   SEQUENCE   814 AA;  91379 MW;  162CDD52590D1A00 CRC64;
     MKLLKFGGTS LANAKKFLCV ADIIEKKNKK EQIAVVLSAP AKITNYLATI IENKIDDEVL
     KKINLAKNIF IELIQDIKRI QPLFPYENTK STIEIEFNKL KKIINGILLI KQCPEGIKPI
     IISRGEILSV DIMKNILQSR NHEVTILNPV TNLLSIGNYL DSTIDIKESK KRIKKINIDQ
     KNIILMAGFI AGNKEGELVV LGRNGSDYSA AILASCLNAK CCEIWTDVDG VLTADPRIVS
     NTYLLDYISY QEAMELSYFG AKVLHPRTIE PISQFQIPCV IKNTNNTESK GTWIGKENNP
     SDNSLKGVTY LDNIIMFNIS GSCLKDSGNT IARIFTILSR ESMKIILIIQ SSSENQINFC
     TFEKDIDYIL LILKKEFTLE IKEGLLNDFN IVKNLTILSV IGSNISEKNN IASKIFSSLG
     SSKINVLAIA HGSSKHSISI VIKKENLLQG IQNIHNTLFF KKTIINVFLI GIGGVGKALL
     KQILKQEKFL DQKNIKIQFR MIANSKKLLF LKNSINLNNW EENFKKSKEK FNLTILNELL
     KNTCDSNSVI IDCTSDYILS KQYISFIKKG FHIITSNKKA NTDSLKYYSE IRTTALKENK
     KFLYETNVGA GLPVINTLQS LFSTGDCLIS FKGILSGSLS FIFGKLEEGV LLSEATKEAK
     KLGFTEPNPF DDLSGIDVAR KLLVLAREIG YSIELKDISI EPILPERFKK YQNSEEFLFK
     LKELDSFFSE RVNKARDIGN VLRFIGSIEK NGKCSVKIEE INSNNPLYKV KNGENALTFY
     TNYYQPIPLV LRGYGAGNDV TASGVFSDLL RIIL
//