ID   AKH_BUCAI               Reviewed;         816 AA.
AC   P57290;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   04-NOV-2008, entry version 51.
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=BU194;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (Acyrthosiphon pisum
OS   symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=118099;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tokyo 1998;
RX   MEDLINE=20445173; PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids
RT   Buchnera sp. APS.";
RL   Nature 407:81-86(2000).
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.
CC   -!- SIMILARITY: Contains 2 ACT domains.
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DR   EMBL; BA000003; BAB12911.1; -; Genomic_DNA.
DR   RefSeq; NP_240025.1; -.
DR   HSSP; P31116; 1EBF.
DR   GeneID; 1109637; -.
DR   GenomeReviews; BA000003_GR; BU194.
DR   KEGG; buc:BU194; -.
DR   HOGENOM; P57290; -.
DR   BioCyc; BSP107806:BU194-MON; -.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR002912; ACT_bd.
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; PF01842; ACT; 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_0000066684.
FT   DOMAIN      398    468       ACT.
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;  91809 MW;  CEACE5C565465884 CRC64;
     MKLLKFGGTS LANAEKFLSV SSIIEENTQT DQIAVVLSAP AKITNYLVKI IENTIKNNQI
     LETVHLAENI FMQLINNFLN IQSNFPHKEI EKIIKKEFNE LKNIIQGILL LKQCPDNIRA
     IIISRGEILS VFIMKSILQS KNYNVTIINP VKNLVAIGDN YLDSTVDISE SKKNIQNMNI
     NQSNIILMAG FIAGNKDKKL VVLGRNGSDY SAAVLAACLD ANCCEIWTDV DGVFTSDPRK
     VPNARLLKSI SYQEAMELSY FGAKVLHPRT IEPIAQFKIP CLIKNTNNVK SIGTLICEQN
     CSEKDFLKGV THLDEIAMFN ISGPHIKDVG SVISRIFTMM SRGNIKILLI TQSSSENKIN
     FCVYEHDIYK ILYLFNKEFQ LELKDGLLNP FKIKKNLSIL SIVGSNIYKK HNIASKIFSV
     LGALKINVIA ISQGSSKHSI SLVIKKENIL KAVQHVHNTL FFNKKTIHMF LIGIGGIGST
     LLNQILKQKQ FLDKKNIEIK ICAIANSKKI LLLDNTNDLS NWKNDFKKST QKFNLELLNN
     LIKNNHFSNS VIVDCTSSQL LSEQYVNFID NNFHVVTSNK KANTSEWNYY KKIRKSVAQT
     GKKFLYETNV GAGLPVIETL QNLFKSGDNL ICFKGILSGS LSFIFGRLEE GILLSQATRE
     AKELGFTEPN PCDDLSGIDV ARKLLILARE SGYNIELKDI KIEPLLPNNF KIYEDTDKFL
     LKLKELDVYF SNKIKQALNV GNVLRFVATI EQKRQFFIKL EEVNINNPLY KVKNGENALA
     FYTNYYQPIP LVLRGYGAGN NVTASGVFSD LLRTLS
//