ID A0A0W0YWI6_9GAMM Unreviewed; 803 AA.
AC A0A0W0YWI6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=lysAC_2 {ECO:0000313|EMBL:KTD61285.1};
GN ORFNames=Lsha_1258 {ECO:0000313|EMBL:KTD61285.1};
OS Legionella shakespearei DSM 23087.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1122169 {ECO:0000313|EMBL:KTD61285.1, ECO:0000313|Proteomes:UP000054600};
RN [1] {ECO:0000313|EMBL:KTD61285.1, ECO:0000313|Proteomes:UP000054600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49655 {ECO:0000313|EMBL:KTD61285.1,
RC ECO:0000313|Proteomes:UP000054600};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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 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}.
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:KTD61285.1}.
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DR EMBL; LNYW01000038; KTD61285.1; -; Genomic_DNA.
DR RefSeq; WP_018578174.1; NZ_LNYW01000038.1.
DR AlphaFoldDB; A0A0W0YWI6; -.
DR STRING; 1122169.Lsha_1258; -.
DR PATRIC; fig|1122169.6.peg.1456; -.
DR eggNOG; COG0460; Bacteria.
DR eggNOG; COG0527; Bacteria.
DR OrthoDB; 9799110at2; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000054600; Unassembled WGS sequence.
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; cd04921; ACT_AKi-HSDH-ThrA-like_1; 1.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.2130.10; VC0802-like; 2.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR045865; ACT-like_dom_sf.
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; 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; 2.
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; 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|PIRNR:PIRNR000727};
KW Kinase {ECO:0000256|PIRNR:PIRNR000727, ECO:0000313|EMBL:KTD61285.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000727};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000727};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000727};
KW Reference proteome {ECO:0000313|Proteomes:UP000054600};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697};
KW Transferase {ECO:0000256|PIRNR:PIRNR000727, ECO:0000313|EMBL:KTD61285.1}.
FT DOMAIN 1..271
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
FT DOMAIN 299..359
FT /note="CASTOR ACT"
FT /evidence="ECO:0000259|Pfam:PF13840"
FT DOMAIN 383..443
FT /note="CASTOR ACT"
FT /evidence="ECO:0000259|Pfam:PF13840"
FT DOMAIN 459..594
FT /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF03447"
FT DOMAIN 602..797
FT /note="Homoserine dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00742"
SQ SEQUENCE 803 AA; 88174 MW; 59DE3EB41D1CFB48 CRC64;
MTVVNKLGGS CLRSVDDYLQ IHRIVRDTPC ILVVSASNGT TRKLYDCLSI ASKRQNYMPY
LDEVIQSHYL LNQQLTNDEQ IQNSILKDKE DIISLLHSIT LLGDYSEEQK NWLLGYGEYW
SSKIIAGLLA APWIDAGQII TVKLHEGVVH IDWKETRKRW NKALKGINAP VLVLPGFVAR
DNRGLRALLG FNGSDFTAAI IAKLIKAKHF CKWTDIDGIY SADPKLVKSA FAIPDLSYQE
AAELAYFGAS VLHPQSVQPA IEANIPIHIK NYFKMDSPGT VISSTPEKTP IIIKGLSSIC
DLALINIEGT GLVGLCGVAG RLFQSLAKAD ISVILISQAS SEHSISIVVK EEQGEDAVQQ
IKHEFDFELA HGIIQNVALL NQCTVVSAVG DRMCGTPGVA AKFFEMLHKA NINILAIAQG
SSQRSLSAVI DQKVTQRALQ VLHGGFYLSR KTLSIGLIGP GGVGAEFLDQ IKKNCLRLKS
ELNVDLKVRG IMNSKSMLLY DTAFDLYDWQ ASMATDSTGK NIKDFIHHVA SPEIPHAVII
DCTSSADVAK QYQSFIDQGC HIVTPNKKAN SSDLEEYKKL KSHVQANNRH YLYETTVCAG
LPVIKTIQDL LATGDTVKRI EGIVSGTLSY IFHQCARGIS FADSVKQAYD LGYTEPDPRE
DLNGLDVARK FVCLARELGY DAALEDVTLL NMVPKELKDV SITDFLNKLP EHQKSIEDKI
KKLVQDNAAV AYVGIIENGK IMIQLNAYPA SHPFANTTGT DNILLIQSRR YDKQPLIIQG
PGAGQDVTAA GVFADLLKLA SML
//
