ID   AKH_HAEIN               Reviewed;         815 AA.
AC   P44505;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   04-NOV-2008, entry version 61.
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=HI0089;
OS   Haemophilus influenzae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=727;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   MEDLINE=95350630; PubMed=7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M.,
RA   Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
RA   Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
RA   Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
RA   Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
RA   Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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; L42023; AAC21767.1; -; Genomic_DNA.
DR   PIR; A64048; A64048.
DR   RefSeq; NP_438262.1; -.
DR   HSSP; P31116; 1EBF.
DR   GeneID; 950991; -.
DR   GenomeReviews; L42023_GR; HI0089.
DR   KEGG; hin:HI0089; -.
DR   NMPDR; fig|71421.1.peg.88; -.
DR   TIGR; HI0089; -.
DR   HOGENOM; P44505; -.
DR   BioCyc; HINF71421:HI_0089-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; 2.
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   Allosteric enzyme; Amino-acid biosynthesis; Complete proteome; Kinase;
KW   Multifunctional enzyme; NADP; Oxidoreductase; Repeat;
KW   Threonine biosynthesis; Transferase.
FT   CHAIN         1    815       Bifunctional aspartokinase/homoserine
FT                                dehydrogenase.
FT                                /FTId=PRO_0000066687.
FT   DOMAIN      316    390       ACT 1.
FT   DOMAIN      397    471       ACT 2.
FT   NP_BIND     471    478       NADP (Potential).
FT   REGION        1    249       Aspartokinase.
FT   REGION      250    470       Interface.
FT   REGION      471    815       Homoserine dehydrogenase.
SQ   SEQUENCE   815 AA;  88221 MW;  7FD5512FCC4BE7F7 CRC64;
     MRVLKFGGTS LANPERFSQA AKLIEQAHLE EQAAGVLSAP AKITNHLVAL SEKAALNQST
     DTHFNEAIEI FYNIINGLHT ENNQFDLNGT KALIDAEFVQ IKGLLEEIRQ AGKVEDAVKA
     TIDCRGEKLS IAMMKAWFEA RGYSVHIVDP VKQLLAKGGY LESSVEIEES TKRVDAANIA
     KDKVVLMAGF TAGNEKGELV LLGRNGSDYS AACLAACLGA SVCEIWTDVD GVYTCDPRLV
     PDARLLPTLS YREAMELSYF GAKVIHPRTI GPLLPQNIPC VIKNTGNPSA PGSIIDGNVK
     SESLQVKGIT NLDNLAMFNV SGPGMQGMVG MASRVFSAMS GAGISVILIT QSSSEYSISF
     CVPVKSAEVA KTVLETEFAN ELNEHQLEPI EVIKDLSIIS VVGDGMKQAK GIAARFFSAL
     AQANISIVAI AQGSSERSIS AVVPQNKAIE AVKATHQALF NNKKVVDMFL VGVGGVGGEL
     IEQVKRQKEY LAKKNVEIRV CAIANSNRML LDENGLNLED WKNDLENATQ PSDFDVLLSF
     IKLHHVVNPV FVDCTSAESV AGLYARALKE GFHVVTPNKK ANTRELVYYN ELRQNAQASQ
     HKFLYETNVG AGLPVIENLQ NLLAAGDELE YFEGILSGSL SFIFGKLEEG LSLSEVTALA
     REKGFTEPDP RDDLSGQDVA RKLLILAREA GIELELSDVE VEGVLPKGFS DGKSADEFMA
     MLPQLDEEFK TRVATAKAEG KVLRYVGKIS EGKCKVSIVA VDLNNPLYKV KDGENALAFY
     TRYYQPIPLL LRGYGAGNAV TAAGIFADIL RTLQH
//