ID   AK1H_SERMA              Reviewed;         819 AA.
AC   P27725; Q59936; Q59937; Q60127; Q60157;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   04-NOV-2008, entry version 64.
DE   RecName: Full=Bifunctional aspartokinase/homoserine dehydrogenase 1;
DE   AltName: Full=Aspartokinase I/homoserine dehydrogenase I;
DE            Short=AKI-HDI;
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; Synonyms=thrA1, thrA2;
OS   Serratia marcescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Serratia.
OX   NCBI_TaxID=615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sr41 / 8000, Sr41 / HNr21, Sr41 / HNr59, and Sr41 / TLr156;
RX   MEDLINE=93139048; PubMed=8423151;
RA   Omori K., Suzuki S., Komatsubara S.;
RT   "Nucleotide sequence of the Serratia marcescens threonine operon and
RT   analysis of the threonine operon mutations which alter feedback
RT   inhibition of both aspartokinase I and homoserine dehydrogenase I.";
RL   J. Bacteriol. 175:785-794(1993).
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   -!- ENZYME REGULATION: The enzyme activities are regulated
CC       allosterically by L-threonine.
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.
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; D10385; BAA38474.1; -; Genomic_DNA.
DR   EMBL; D10386; BAA38477.1; -; Genomic_DNA.
DR   EMBL; D10387; BAA38480.1; -; Genomic_DNA.
DR   EMBL; X60821; CAA43212.1; -; Genomic_DNA.
DR   PIR; B47057; B47057.
DR   HSSP; P31116; 1EBF.
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; Kinase;
KW   Multifunctional enzyme; NADP; Oxidoreductase; Repeat;
KW   Threonine biosynthesis; Transferase.
FT   CHAIN         1    819       Bifunctional aspartokinase/homoserine
FT                                dehydrogenase 1.
FT                                /FTId=PRO_0000066682.
FT   DOMAIN      316    385       ACT 1.
FT   DOMAIN      397    468       ACT 2.
FT   NP_BIND     471    478       NADP (Potential).
FT   REGION        1    249       Aspartokinase (By similarity).
FT   REGION      250    470       Interface (By similarity).
FT   REGION      471    819       Homoserine dehydrogenase (By similarity).
FT   VARIANT     330    330       G -> D (in strain: Sr41 / 8000, Sr41 /
FT                                HNr21; loss of feedback inhibition).
FT   VARIANT     352    352       S -> F (in strain: Sr41 / TLr156; loss of
FT                                feedback inhibition).
FT   VARIANT     479    479       A -> T (in strain: Sr41 / HNr59; Thr-
FT                                resistant HDI).
SQ   SEQUENCE   819 AA;  88495 MW;  1F18552B036A8E39 CRC64;
     MRVLKFGGTS VANAERFLRV ADIMESNARQ GQVATVLSAP AKITNHLVAM IDKTVAGQDI
     LPNMSDAERI FADLLSGLAQ ALPGFEYDRL KGVVDQEFAQ LKQVLHGVSL LGQCPDSVNA
     AIICRGEKLS IAIMEGVFRA KGYPVTVINP VEKLLAQGHY LESTVDIAES TLRIAAAAIP
     ADHIVLMAGF TAGNDKGELV VLGRNGSDYS AAVLAACLRA DCCEIWTDVD GVYTCDPRTV
     PDARLLKSMS YQEAMELSYF GAKVLHPRTI TPIAQFQIPC LIKNTSNPQA PGTLIGKDST
     DADMPVKGIT NLNNMAMINV SGPGMKGMVG MAARVFAVMS RAGISVVLIT QSSSEYSISF
     CVPQGELQRA RRALEEEFYL ELKDGVLDPL DVMERLAIIS VVGDGMRTLR GISARFFSAL
     ARANINIVAI AQGSSERSIS VVVSNDSATT GVRVSHQMLF NTDQVIEVFV IGVGGVGGAL
     IEQIYRQQPW LKQKHIDLRV CGIANSRVML TNVHGIALDS WRDALAGAQE PFNLGRLIRL
     VKEYHLLNPV IVDCTSSQAV ADQYVDFLAD GFHVVTPNKK ANTSSMNYYQ QLRAAAAGSH
     RKFLYDTNVG AGLPVIENLQ NLLNAGDELV RFSGILSGSL SFIFGKLDEG LSLSAATLQA
     RANGYTEPDP RDDLSGMDVA RKLLILAREA GYKLELSDIE VEPVLPPSFD ASGDVDTFLA
     RLPELDKEFA RNVANAAEQG KVLRYVGLID EGRCKVRIEA VDGNDPLYKV KNGENALAFY
     SRYYQPLPLV LRGYGAGNDV TAAGVFADLL RTLSWKLGV
//