ID   AKH_BUCBP               Reviewed;         816 AA.
AC   Q89AR4;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   22-JUL-2008, entry version 38.
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=bbp_183;
OS   Buchnera aphidicola subsp. Baizongia pistaciae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=135842;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22426901; PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO26915.1; -; Genomic_DNA.
DR   RefSeq; NP_777810.1; -.
DR   HSSP; P31116; 1EBF.
DR   GeneID; 1058230; -.
DR   GenomeReviews; AE016826_GR; bbp_183.
DR   KEGG; bab:bbp183; -.
DR   HOGENOM; Q89AR4; -.
DR   BioCyc; BAPH224915:BBP_183-MON; -.
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    816       Bifunctional aspartokinase/homoserine
FT                                dehydrogenase.
FT                                /FTId=PRO_0000066686.
FT   NP_BIND     472    479       NADP (Potential).
FT   REGION        1    250       Aspartokinase (By similarity).
FT   REGION      251    471       Interface (By similarity).
FT   REGION      472    816       Homoserine dehydrogenase (By similarity).
SQ   SEQUENCE   816 AA;  91919 MW;  F8C3ADC0114576B5 CRC64;
     MKILKFGGTS LSNSELFFHV ATIIENNLNN EQIAIVLSAP GNTTNLLEIA INQTINNKNI
     IPIVQKIEKN FLKLINDIYQ VEQKLLYEKI KNNIENKLLE LKNLLQGINL LRQCPDKIRA
     KIISSGEYLS ISIMNSILIS RGYNTTIIDP VKKLLTKEDT YLNATVNIKI SKFRILSMKI
     PKHHIILMPG FTAGNKQGEL VTLGRNGSDY SATILSVCLN STMCEIWTDV NGVYTCDPKL
     VSDAKLLTSL SYREAIELSY LGAKILHPNT IYPIQKFKIP CTIKNTHNPS SIGTKISCNH
     VKNKNLITGV TYLENVHMFS ISCLYSKNIE TIIPKIFSCM SLSKIWIILT IQTSSQNTIS
     FCILKTMTNT ALHVLHKALY LELKHKLLKP IKVEKKLTLI SVISSDILNN TKITEKVFSI
     LKHVNINTLA ISKGASKNSI SIVVKHDDGI LGVRALHKGI FNKNCTAEIF LIGIGRVGQT
     FLKQIIEQKN WLKSKNIDLK ICGIANSKNF ILNLDGINPK NWKRDLNLSK KSFNFKHLLN
     SIQNYYLINP IIVDCTSDKN IANQYISFIN CGFHIVTPNK KANTTNWKYY EDIRLAAQKE
     KKKFFYETNV GAGLPVIENL KNLLRTGDTL IHFKGILSGS LSFIFGKLED NISLSEATKQ
     AQSLGFTEPN PKDDLSGIDV ARKLLILARE VGYKLELKDI KIEPLLPKEF NNISNTTDFI
     TKLKELDQIF CNRVKKARKL GKRLRFVGII NQKGNCQVKI DEVDHNDPLY NIKNGENALA
     FYSKYYQPIP LVLRGYGAGN NVTASGIFSD VLRILL
//