AKH_BUCBP
ID AKH_BUCBP Reviewed; 816 AA.
AC Q89AR4;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=bbp_183;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO26915.1; -; Genomic_DNA.
DR RefSeq; WP_011091316.1; NC_004545.1.
DR AlphaFoldDB; Q89AR4; -.
DR SMR; Q89AR4; -.
DR STRING; 224915.bbp_183; -.
DR PRIDE; Q89AR4; -.
DR EnsemblBacteria; AAO26915; AAO26915; bbp_183.
DR GeneID; 56470725; -.
DR KEGG; bab:bbp_183; -.
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; UP000000601; 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; 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; 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_0000066686"
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; 91919 MW; F8C3ADC0114576B5 CRC64;
MKILKFGGTS LSNSELFFHV ATIIENNLNN EQIAIVLSAP GNTTNLLEIA INQTINNKNI
IPIVQKIEKN FLKLINDIYQ VEQKLLYEKI KNNIENKLLE LKNLLQGINL LRQCPDKIRA
KIISSGEYLS ISIMNSILIS RGYNTTIIDP VKKLLTKEDT YLNATVNIKI SKFRILSMKI
PKHHIILMPG FTAGNKQGEL VTLGRNGSDY SATILSVCLN STMCEIWTDV NGVYTCDPKL
VSDAKLLTSL SYREAIELSY LGAKILHPNT IYPIQKFKIP CTIKNTHNPS SIGTKISCNH
VKNKNLITGV TYLENVHMFS ISCLYSKNIE TIIPKIFSCM SLSKIWIILT IQTSSQNTIS
FCILKTMTNT ALHVLHKALY LELKHKLLKP IKVEKKLTLI SVISSDILNN TKITEKVFSI
LKHVNINTLA ISKGASKNSI SIVVKHDDGI LGVRALHKGI FNKNCTAEIF LIGIGRVGQT
FLKQIIEQKN WLKSKNIDLK ICGIANSKNF ILNLDGINPK NWKRDLNLSK KSFNFKHLLN
SIQNYYLINP IIVDCTSDKN IANQYISFIN CGFHIVTPNK KANTTNWKYY EDIRLAAQKE
KKKFFYETNV GAGLPVIENL KNLLRTGDTL IHFKGILSGS LSFIFGKLED NISLSEATKQ
AQSLGFTEPN PKDDLSGIDV ARKLLILARE VGYKLELKDI KIEPLLPKEF NNISNTTDFI
TKLKELDQIF CNRVKKARKL GKRLRFVGII NQKGNCQVKI DEVDHNDPLY NIKNGENALA
FYSKYYQPIP LVLRGYGAGN NVTASGIFSD VLRILL
