AKH_BUCAP
ID AKH_BUCAP Reviewed; 814 AA.
AC Q8K9U9;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=BUsg_188;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
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; AE013218; AAM67753.1; -; Genomic_DNA.
DR RefSeq; WP_011053720.1; NC_004061.1.
DR AlphaFoldDB; Q8K9U9; -.
DR SMR; Q8K9U9; -.
DR STRING; 198804.BUsg_188; -.
DR PRIDE; Q8K9U9; -.
DR EnsemblBacteria; AAM67753; AAM67753; BUsg_188.
DR KEGG; bas:BUsg_188; -.
DR eggNOG; COG0460; Bacteria.
DR eggNOG; COG0527; Bacteria.
DR HOGENOM; CLU_009116_7_1_6; -.
DR OMA; CNKIACS; -.
DR OrthoDB; 1067792at2; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000000416; 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; Threonine biosynthesis; Transferase.
FT CHAIN 1..814
FT /note="Bifunctional aspartokinase/homoserine dehydrogenase"
FT /id="PRO_0000066685"
FT DOMAIN 319..400
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT REGION 1..248
FT /note="Aspartokinase"
FT /evidence="ECO:0000250"
FT REGION 249..469
FT /note="Interface"
FT /evidence="ECO:0000250"
FT REGION 470..814
FT /note="Homoserine dehydrogenase"
FT /evidence="ECO:0000250"
FT BINDING 470..477
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
SQ SEQUENCE 814 AA; 91379 MW; 162CDD52590D1A00 CRC64;
MKLLKFGGTS LANAKKFLCV ADIIEKKNKK EQIAVVLSAP AKITNYLATI IENKIDDEVL
KKINLAKNIF IELIQDIKRI QPLFPYENTK STIEIEFNKL KKIINGILLI KQCPEGIKPI
IISRGEILSV DIMKNILQSR NHEVTILNPV TNLLSIGNYL DSTIDIKESK KRIKKINIDQ
KNIILMAGFI AGNKEGELVV LGRNGSDYSA AILASCLNAK CCEIWTDVDG VLTADPRIVS
NTYLLDYISY QEAMELSYFG AKVLHPRTIE PISQFQIPCV IKNTNNTESK GTWIGKENNP
SDNSLKGVTY LDNIIMFNIS GSCLKDSGNT IARIFTILSR ESMKIILIIQ SSSENQINFC
TFEKDIDYIL LILKKEFTLE IKEGLLNDFN IVKNLTILSV IGSNISEKNN IASKIFSSLG
SSKINVLAIA HGSSKHSISI VIKKENLLQG IQNIHNTLFF KKTIINVFLI GIGGVGKALL
KQILKQEKFL DQKNIKIQFR MIANSKKLLF LKNSINLNNW EENFKKSKEK FNLTILNELL
KNTCDSNSVI IDCTSDYILS KQYISFIKKG FHIITSNKKA NTDSLKYYSE IRTTALKENK
KFLYETNVGA GLPVINTLQS LFSTGDCLIS FKGILSGSLS FIFGKLEEGV LLSEATKEAK
KLGFTEPNPF DDLSGIDVAR KLLVLAREIG YSIELKDISI EPILPERFKK YQNSEEFLFK
LKELDSFFSE RVNKARDIGN VLRFIGSIEK NGKCSVKIEE INSNNPLYKV KNGENALTFY
TNYYQPIPLV LRGYGAGNDV TASGVFSDLL RIIL
