AKH_BUCAI
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 03-AUG-2022, entry version 130.
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 (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX 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 Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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 -!- 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. {ECO:0000250}.
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; BA000003; BAB12911.1; -; Genomic_DNA.
DR RefSeq; NP_240025.1; NC_002528.1.
DR RefSeq; WP_010895993.1; NC_002528.1.
DR AlphaFoldDB; P57290; -.
DR SMR; P57290; -.
DR STRING; 107806.10038876; -.
DR PRIDE; P57290; -.
DR EnsemblBacteria; BAB12911; BAB12911; BAB12911.
DR KEGG; buc:BU194; -.
DR PATRIC; fig|107806.10.peg.205; -.
DR eggNOG; COG0460; Bacteria.
DR eggNOG; COG0527; Bacteria.
DR HOGENOM; CLU_009116_7_1_6; -.
DR OMA; CNKIACS; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000001806; Chromosome.
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; 1.20.120.1320; -; 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; IPR042199; AsparK_Bifunc_asparK/hSer_DH.
DR InterPro; IPR018042; Aspartate_kinase_CS.
DR InterPro; IPR011147; Bifunc_aspartokin/hSer_DH.
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; 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; 1.
DR PROSITE; PS00324; ASPARTOKINASE; 1.
DR PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; ATP-binding; Kinase; Multifunctional enzyme; NADP;
KW Nucleotide-binding; Oxidoreductase; Reference proteome;
KW Threonine biosynthesis; Transferase.
FT CHAIN 1..816
FT /note="Bifunctional aspartokinase/homoserine dehydrogenase"
FT /id="PRO_0000066684"
FT DOMAIN 402..479
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT REGION 1..250
FT /note="Aspartokinase"
FT /evidence="ECO:0000250"
FT REGION 251..471
FT /note="Interface"
FT /evidence="ECO:0000250"
FT REGION 472..816
FT /note="Homoserine dehydrogenase"
FT /evidence="ECO:0000250"
FT BINDING 472..479
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
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
