ID B6EKY8_ALISL Unreviewed; 819 AA.
AC B6EKY8;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Bifunctional aspartokinase/homoserine dehydrogenase {ECO:0000256|PIRNR:PIRNR000727};
DE Includes:
DE RecName: Full=Aspartokinase {ECO:0000256|PIRNR:PIRNR000727};
DE EC=2.7.2.4 {ECO:0000256|PIRNR:PIRNR000727};
DE Includes:
DE RecName: Full=Homoserine dehydrogenase {ECO:0000256|PIRNR:PIRNR000727};
DE EC=1.1.1.3 {ECO:0000256|PIRNR:PIRNR000727};
GN Name=thrA {ECO:0000313|EMBL:CAQ80240.1};
GN OrderedLocusNames=VSAL_I2556 {ECO:0000313|EMBL:CAQ80240.1};
OS Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS LFI1238)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=316275 {ECO:0000313|EMBL:CAQ80240.1, ECO:0000313|Proteomes:UP000001730};
RN [1] {ECO:0000313|EMBL:CAQ80240.1, ECO:0000313|Proteomes:UP000001730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LFI1238 {ECO:0000313|EMBL:CAQ80240.1,
RC ECO:0000313|Proteomes:UP000001730};
RX PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT LFI1238 shows extensive evidence of gene decay.";
RL BMC Genomics 9:616-616(2008).
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 Evidence={ECO:0000256|ARBA:ARBA00000709,
CC ECO:0000256|PIRNR:PIRNR000727};
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 Evidence={ECO:0000256|ARBA:ARBA00001406};
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 Evidence={ECO:0000256|ARBA:ARBA00000116,
CC ECO:0000256|PIRNR:PIRNR000727};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004766, ECO:0000256|PIRNR:PIRNR000727}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 1/3.
CC {ECO:0000256|ARBA:ARBA00004986, ECO:0000256|PIRNR:PIRNR000727}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 3/3.
CC {ECO:0000256|ARBA:ARBA00005062, ECO:0000256|PIRNR:PIRNR000727}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 1/5. {ECO:0000256|ARBA:ARBA00005139,
CC ECO:0000256|PIRNR:PIRNR000727}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 3/5. {ECO:0000256|ARBA:ARBA00005056,
CC ECO:0000256|PIRNR:PIRNR000727}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC ECO:0000256|PIRNR:PIRNR000727}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the homoserine
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007952,
CC ECO:0000256|PIRNR:PIRNR000727}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the aspartokinase
CC family. {ECO:0000256|ARBA:ARBA00010046, ECO:0000256|PIRNR:PIRNR000727}.
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DR EMBL; FM178379; CAQ80240.1; -; Genomic_DNA.
DR RefSeq; WP_012551027.1; NC_011312.1.
DR AlphaFoldDB; B6EKY8; -.
DR KEGG; vsa:VSAL_I2556; -.
DR eggNOG; COG0460; Bacteria.
DR eggNOG; COG0527; Bacteria.
DR HOGENOM; CLU_009116_7_1_6; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000001730; Chromosome 1.
DR GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd04257; AAK_AK-HSDH; 1.
DR CDD; cd04921; ACT_AKi-HSDH-ThrA-like_1; 1.
DR CDD; cd04922; ACT_AKi-HSDH-ThrA_2; 1.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR Gene3D; 1.20.120.1320; Aspartokinase, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.2130.10; VC0802-like; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR049638; AK-HD.
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 NCBIfam; TIGR00657; asp_kinases; 1.
DR PANTHER; PTHR43070; -; 1.
DR PANTHER; PTHR43070:SF3; HOMOSERINE DEHYDROGENASE; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF01842; ACT; 1.
DR Pfam; PF00742; Homoserine_dh; 1.
DR Pfam; PF03447; NAD_binding_3; 1.
DR PIRSF; PIRSF000727; ThrA; 1.
DR SUPFAM; SSF55021; ACT-like; 2.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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 {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|PIRNR:PIRNR000727};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000727};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000727};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000727};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000727};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000727};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000727}.
FT DOMAIN 320..394
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 819 AA; 88607 MW; CD55ADE23B4F1F1E CRC64;
MRVLKFGGSS LADSDRFLRA ADIIANNAQQ QDVSVVLSAP GKVTNKLVSV VDNVLTNGEA
ELQISELEAV FIQLFDGIST ALPQVDLKTL ENKLKDSLSQ LRQYVHGISL LGMCPDNVYA
KIISKGERIS VVTMKAVLEA KGQQASLIDP VKYLYARGSF LEGAVDVDIS TLNFKNEPLP
KGHVNIMPGF TAGNEKGELL TLGRNGSDYS AAVLAACLRA ECCEIWTDVD GVYNCDPRLV
DDARLLKSLS YQEAMELSYF GASVLHPKTI APIAQFHIPC LIKNSFNPQG PGTLIGQDTG
EDNLAIKGIT TLSNLTMVNV SGPGMKGMVG MASRVFGAMS TAGISIVLIT QSSSEYSISF
CIEAEDKVQA EQVLREAFEL ELKDGLLEPV EFINDVAIVT LVGDGMRTSK GVASQFFTSL
TEVNVNIIAI AQGSSERAIS AVIPEDKVSE SIKACHENLF NSKHFLDVFV VGVGGVGGEL
VEQIKRQQPK LSQKGIEIRV CGLANSRGLL LDSKGISLDG WRDRMGNATE EFSLARLISL
VQRNHIINPV IIDCTSDHGI AAQYVDFLSA GFHVITPNKK SNTDSMAYYH QLRNAARATR
RKFMYETTVG AGLPVIENLQ NLIAAGDELV KFNGILSGSM SYIFGKLDEG MSLSDATNVA
KKNGFTEPDP RDDLSGMDVA RKLLILARES GLEIELDDVE VEQALPPGFD DSGTIDEFMA
RLPEADAYFV QESAKAAEEG KVLRYVGEIS EGKCKVRIAA VDGDDPMFKI KDGENALAFY
SRYYQPIPLV LRGYGAGTEV TAAGVFSDLM RTLGWKLGV
//
