ID A0A0G1WH24_9BACT Unreviewed; 818 AA.
AC A0A0G1WH24;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Aspartate kinase {ECO:0000313|EMBL:KKW17940.1};
GN ORFNames=UY60_C0027G0002 {ECO:0000313|EMBL:KKW17940.1};
OS Parcubacteria group bacterium GW2011_GWB1_50_9.
OC Bacteria.
OX NCBI_TaxID=1618884 {ECO:0000313|EMBL:KKW17940.1, ECO:0000313|Proteomes:UP000034442};
RN [1] {ECO:0000313|EMBL:KKW17940.1, ECO:0000313|Proteomes:UP000034442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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-threonine biosynthesis; L-threonine
CC from L-aspartate: step 1/5. {ECO:0000256|ARBA:ARBA00005139}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the aspartokinase family.
CC {ECO:0000256|ARBA:ARBA00010122}.
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:KKW17940.1}.
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DR EMBL; LCQP01000027; KKW17940.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1WH24; -.
DR PATRIC; fig|1618884.3.peg.533; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000034442; Unassembled WGS sequence.
DR GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC.
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 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; 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; PTHR21499; ASPARTATE KINASE; 1.
DR PANTHER; PTHR21499:SF59; ASPARTOKINASE; 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; 2.
DR PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Kinase {ECO:0000313|EMBL:KKW17940.1};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:KKW17940.1}.
FT DOMAIN 309..384
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT DOMAIN 390..458
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 818 AA; 88610 MW; C5D939FDADCC6F19 CRC64;
MGSVESLRKV ISIIKNPQQD GRIVAVIVSA MSGVTDQIIE IGKRAAAKDD SYKKILRALE
DRHVKTAQSL VGRKEQEIAL QHIGVLFDAL ERVARGVFLV REISPGALDY IMSYGERLSA
HILCDALRSR GIKCEYVNAR TLITTDSSFG HAAVDFKTTD KVIRKHFKAN PKMQIVTGFI
ATSPEGKTTT LGRGGSDYTA SIVGAALGVR AIEIWTDVPG VMTADPRKVK DALPVRKLSY
SEAAEMSYFG AKVIHPPTMR PAELRHIPIL IKNTFAPEAP GTVIGSSSLR SEALATGITS
ISDIAILEVE GGGMVSARGA VGRLFSALAR EKVNVVLITQ ASSQNSITIA VAPKDAGHAK
LAIEEEFALE RAANLIDRVE VRTGLSVIAV VGERLRNQPG IAGSMFQMLG KNGINVVVIA
QGSSELNISV VVEQKDEAKA LNAIHTGFFF PKTKYINVFL LGTGLIGGTL LTQIAKQDEF
LKEEYGYVIR IIGLADEGKM IFSSGDGMTL GGDTDGIDPE NWHALLTASG SRMKLHDFID
KMKRIDLPDK VFVDCTASEE VAATYADILK ARISIVAPNK KAASGPMKRY RKIGEFAKMP
GVKFLYETNV GAALPIISTL NDLFLSGDEV LKIEAVLSGS LSYVFNEFTG KRRFSEVVRK
ARAKGYTEPD PREDLSGRDV ARKILILARE TGESMELSDV KVESLVSSLS SKAKTIGGLF
KQLEREDARL EKKKQSALEK GLRLRYIATF EKRKASVSLQ AVPPSHPFYN LSDNDNIVAF
TTKRYNSTPL IVKGPGAGAD VTAAGVFADI LRTARDLV
//
