ID A0A2U2RXT7_9BACT Unreviewed; 817 AA.
AC A0A2U2RXT7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Bifunctional aspartate kinase/homoserine dehydrogenase I {ECO:0000313|EMBL:PWH10662.1};
GN ORFNames=DEJ39_05205 {ECO:0000313|EMBL:PWH10662.1};
OS Bacteroidetes bacterium SCGC AAA795-G10.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=2175803 {ECO:0000313|EMBL:PWH10662.1, ECO:0000313|Proteomes:UP000246014};
RN [1] {ECO:0000313|EMBL:PWH10662.1, ECO:0000313|Proteomes:UP000246014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC AAA795-G10 {ECO:0000313|EMBL:PWH10662.1};
RA Ngugi D.K., Stingl U.;
RT "High-quality draft single-cell genome of the NS5 marine group from the
RT coastal Red Sea.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004766}.
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}.
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}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 1/5. {ECO:0000256|ARBA:ARBA00005139}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 3/5. {ECO:0000256|ARBA:ARBA00005056}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the homoserine
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007952}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the aspartokinase
CC family. {ECO:0000256|ARBA:ARBA00010046}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWH10662.1}.
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DR EMBL; QFDA01000002; PWH10662.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2RXT7; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000246014; Unassembled WGS sequence.
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; cd04243; AAK_AK-HSDH-like; 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; 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 NCBIfam; TIGR00657; asp_kinases; 1.
DR PANTHER; PTHR43070; -; 1.
DR PANTHER; PTHR43070:SF5; HOMOSERINE DEHYDROGENASE; 1.
DR Pfam; PF00696; AA_kinase; 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; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PWH10662.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000246014};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 400..478
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 817 AA; 91069 MW; 4F948761CC3CC3C5 CRC64;
MKVIKFGGTS VANPDSLSLV IDIINRSDEK QLVVVSALSG LTDLLSAMAK NASNSETNYK
ELLNIIEQRH KVLIDHFIPV TKQSEIISFL KAQINELEEI LDSLFKLNEL TSKSKSKILS
FGEILSSNII FKILKYNGND IIFKDTREII FKKTVNDREV VDDFLSKKKT ISFLKKNKHK
ITLFPGFIAS DVEGNTLTLG RGGSDLTASL LANYSDASQL EIWSDVSGMF TANPKLVSQA
TPIRKLSYQE AMELSHFGAK VLYPPTLQPL IKKGIPVNIK NTFDSNARGT RIDRKGSKKS
DGQIVKGVSH IENVALVSLE GSGMIGIPGF SKRLFQTLSD KQINIIMITQ ASSEHSICIG
VKLEDADLSK KLIDENFALE INLQKVEPAK IEKNMTNIAI VGDKMKEHQG ISGKLFSSLG
ANNINIRAIA QGASERNISI LIDKKNTQKA LNTIHESFFE EQIKELNLFV TGVGNVGGKL
LEQLFGQQDY LLKNLRLKIR VISISNSRKM ILSENPINLE TWKDSLENIG IKANREKFFN
HIKKLNLRNS IFIDNTASEE IAEEYVSYLK NSIGVVTCNK IACASSFKNY NNLKKTARRF
VTPFLFETNV GAALPIIDTL NNLIASGDKI LEIQAILSGS LNYIFNNYKL DTTFKNIVQK
AQKEGYTEPD PKIDLSGIDV ARKILILGRE SGFKLELDDI TNNSFIPEEV LKSNNNDELY
KSIDRNENHF RSILERAIKK NKRLKYVAEL KNGKASVGLR EIDENHSFYN LKGSDNIILF
YTSRYKEQPL IVKGAGAGAD VTAGGIFGDI IRIGKTQ
//
