AKH_HAEIN
ID AKH_HAEIN Reviewed; 815 AA.
AC P44505;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 148.
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=HI_0089;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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; L42023; AAC21767.1; -; Genomic_DNA.
DR PIR; A64048; A64048.
DR RefSeq; NP_438262.1; NC_000907.1.
DR RefSeq; WP_005693830.1; NC_000907.1.
DR AlphaFoldDB; P44505; -.
DR SMR; P44505; -.
DR STRING; 71421.HI_0089; -.
DR EnsemblBacteria; AAC21767; AAC21767; HI_0089.
DR KEGG; hin:HI_0089; -.
DR PATRIC; fig|71421.8.peg.90; -.
DR eggNOG; COG0460; Bacteria.
DR eggNOG; COG0527; Bacteria.
DR HOGENOM; CLU_009116_7_1_6; -.
DR OMA; CNKIACS; -.
DR PhylomeDB; P44505; -.
DR BioCyc; HINF71421:G1GJ1-94-MON; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0004072; F:aspartate kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004412; F:homoserine dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0009090; P:homoserine biosynthetic process; IBA:GO_Central.
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 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; 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; 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;
KW Reference proteome; Repeat; Threonine biosynthesis; Transferase.
FT CHAIN 1..815
FT /note="Bifunctional aspartokinase/homoserine dehydrogenase"
FT /id="PRO_0000066687"
FT DOMAIN 320..392
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 REGION 250..470
FT /note="Interface"
FT REGION 471..815
FT /note="Homoserine dehydrogenase"
FT BINDING 471..478
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
SQ SEQUENCE 815 AA; 88221 MW; 7FD5512FCC4BE7F7 CRC64;
MRVLKFGGTS LANPERFSQA AKLIEQAHLE EQAAGVLSAP AKITNHLVAL SEKAALNQST
DTHFNEAIEI FYNIINGLHT ENNQFDLNGT KALIDAEFVQ IKGLLEEIRQ AGKVEDAVKA
TIDCRGEKLS IAMMKAWFEA RGYSVHIVDP VKQLLAKGGY LESSVEIEES TKRVDAANIA
KDKVVLMAGF TAGNEKGELV LLGRNGSDYS AACLAACLGA SVCEIWTDVD GVYTCDPRLV
PDARLLPTLS YREAMELSYF GAKVIHPRTI GPLLPQNIPC VIKNTGNPSA PGSIIDGNVK
SESLQVKGIT NLDNLAMFNV SGPGMQGMVG MASRVFSAMS GAGISVILIT QSSSEYSISF
CVPVKSAEVA KTVLETEFAN ELNEHQLEPI EVIKDLSIIS VVGDGMKQAK GIAARFFSAL
AQANISIVAI AQGSSERSIS AVVPQNKAIE AVKATHQALF NNKKVVDMFL VGVGGVGGEL
IEQVKRQKEY LAKKNVEIRV CAIANSNRML LDENGLNLED WKNDLENATQ PSDFDVLLSF
IKLHHVVNPV FVDCTSAESV AGLYARALKE GFHVVTPNKK ANTRELVYYN ELRQNAQASQ
HKFLYETNVG AGLPVIENLQ NLLAAGDELE YFEGILSGSL SFIFGKLEEG LSLSEVTALA
REKGFTEPDP RDDLSGQDVA RKLLILAREA GIELELSDVE VEGVLPKGFS DGKSADEFMA
MLPQLDEEFK TRVATAKAEG KVLRYVGKIS EGKCKVSIVA VDLNNPLYKV KDGENALAFY
TRYYQPIPLL LRGYGAGNAV TAAGIFADIL RTLQH
