AK1H_SERMA
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 03-AUG-2022, entry version 132.
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; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sr41 / 8000, Sr41 / HNr21, Sr41 / HNr59, and Sr41 / TLr156;
RX PubMed=8423151; DOI=10.1128/jb.175.3.785-794.1993;
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 inhibition
RT of both aspartokinase I and homoserine dehydrogenase I.";
RL J. Bacteriol. 175:785-794(1993).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4-semialdehyde +
CC NADPH; Xref=Rhea:RHEA:15761, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.1.1.3;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde +
CC NADH; Xref=Rhea:RHEA:15757, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:537519; EC=1.1.1.3;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-aspartate = 4-phospho-L-aspartate + ADP;
CC Xref=Rhea:RHEA:23776, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57535, ChEBI:CHEBI:456216; EC=2.7.2.4;
CC -!- ACTIVITY REGULATION: The enzyme activities are regulated allosterically
CC by L-threonine.
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 1/3.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 3/3.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 1/5.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 3/5.
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: In the N-terminal section; belongs to the aspartokinase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the homoserine
CC dehydrogenase family. {ECO:0000305}.
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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 RefSeq; WP_033641811.1; NZ_WUUW01000008.1.
DR AlphaFoldDB; P27725; -.
DR SMR; P27725; -.
DR STRING; 273526.SMDB11_0001; -.
DR PRIDE; P27725; -.
DR GeneID; 64310062; -.
DR PATRIC; fig|615.103.peg.1275; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR UniPathway; UPA00051; UER00465.
DR GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04257; AAK_AK-HSDH; 1.
DR Gene3D; 3.40.1160.10; -; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR041743; AK-HSDH_N.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR InterPro; IPR001341; Asp_kinase.
DR InterPro; IPR018042; Aspartate_kinase_CS.
DR InterPro; IPR011147; Bifunc_aspartokin/hSer_DH.
DR InterPro; IPR027795; CASTOR_ACT_dom.
DR InterPro; IPR001342; HDH_cat.
DR InterPro; IPR019811; HDH_CS.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43070; PTHR43070; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF01842; ACT; 1.
DR Pfam; PF13840; ACT_7; 1.
DR Pfam; PF00742; Homoserine_dh; 1.
DR Pfam; PF03447; NAD_binding_3; 1.
DR PIRSF; PIRSF000727; ThrA; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53633; SSF53633; 1.
DR SUPFAM; SSF55021; SSF55021; 2.
DR TIGRFAMs; TIGR00657; asp_kinases; 1.
DR PROSITE; PS51671; ACT; 2.
DR PROSITE; PS00324; ASPARTOKINASE; 1.
DR PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; Amino-acid biosynthesis; ATP-binding; Kinase;
KW Multifunctional enzyme; NADP; Nucleotide-binding; Oxidoreductase; Repeat;
KW Threonine biosynthesis; Transferase.
FT CHAIN 1..819
FT /note="Bifunctional aspartokinase/homoserine dehydrogenase
FT 1"
FT /id="PRO_0000066682"
FT DOMAIN 320..394
FT /note="ACT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT DOMAIN 401..478
FT /note="ACT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT REGION 1..249
FT /note="Aspartokinase"
FT /evidence="ECO:0000250"
FT REGION 250..470
FT /note="Interface"
FT /evidence="ECO:0000250"
FT REGION 471..819
FT /note="Homoserine dehydrogenase"
FT /evidence="ECO:0000250"
FT BINDING 471..478
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT VARIANT 330
FT /note="G -> D (in strain: Sr41 / 8000, Sr41 / HNr21; loss
FT of feedback inhibition)"
FT VARIANT 352
FT /note="S -> F (in strain: Sr41 / TLr156; loss of feedback
FT inhibition)"
FT VARIANT 479
FT /note="A -> T (in strain: Sr41 / HNr59; Thr-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
