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Database: UniProt
Entry: G8TK81_NIAKG
LinkDB: G8TK81_NIAKG
Original site: G8TK81_NIAKG 
ID   G8TK81_NIAKG            Unreviewed;       816 AA.
AC   G8TK81;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   SubName: Full=Aspartate kinase {ECO:0000313|EMBL:AEV96515.1};
DE            EC=2.7.2.4 {ECO:0000313|EMBL:AEV96515.1};
GN   OrderedLocusNames=Niako_0114 {ECO:0000313|EMBL:AEV96515.1};
OS   Niastella koreensis (strain DSM 17620 / KACC 11465 / NBRC 106392 /
OS   GR20-10).
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Niastella.
OX   NCBI_TaxID=700598 {ECO:0000313|EMBL:AEV96515.1, ECO:0000313|Proteomes:UP000005438};
RN   [1] {ECO:0000313|EMBL:AEV96515.1, ECO:0000313|Proteomes:UP000005438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17620 / KACC 11465 / NBRC 106392 / GR20-10
RC   {ECO:0000313|Proteomes:UP000005438};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Davenport K.,
RA   Saunders E., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA   Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Niastella koreensis GR20-10.";
RL   Submitted (DEC-2011) 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}.
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DR   EMBL; CP003178; AEV96515.1; -; Genomic_DNA.
DR   RefSeq; WP_014216429.1; NC_016609.1.
DR   AlphaFoldDB; G8TK81; -.
DR   STRING; 700598.Niako_0114; -.
DR   KEGG; nko:Niako_0114; -.
DR   PATRIC; fig|700598.3.peg.120; -.
DR   eggNOG; COG0460; Bacteria.
DR   eggNOG; COG0527; Bacteria.
DR   HOGENOM; CLU_009116_7_1_10; -.
DR   OMA; CNKIACS; -.
DR   OrthoDB; 9799110at2; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000005438; Chromosome.
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; 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:AEV96515.1};
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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AEV96515.1}.
FT   DOMAIN          403..481
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   816 AA;  88960 MW;  43952AF68CAC66A8 CRC64;
     MQVLKFGGTS VANAENMNKV SSIVQQALVR MPQSKTIVVV SALGGVTDVL LQSGGLAAAG
     DESYKELLQK VEQRHLEAVK ALIPVTQQSS VLSWVKQRCN EIEDICNGVF LLGELSTRTK
     DRIVSFGELL SSKIIAARLH AQGVENTWVD SRELIRTDSH YGSAVVDFTV TNSLCSNFFS
     VAASRLFIVP GFVAADAHGN TTTLGRGGSD YTAAIIAGAV SAQTLEIWTD VSGMMTADPR
     LVPNAKILPH ISYQEAMELS HFGAKVIYPP TIQPVMSKNI PVWIKNTFAP EDHGTVIEND
     IHKNGNNIRG ISSINKIALL SLEGSGMIGI PGFSRRLFES LANDFINVIL ITQGSSEHSI
     CVGIDEALAG KAKQAVDKTF AYEIEMGRVE PLRVETGLAI VALVGDNMKS HPGISGKMFG
     AIGRNGVNIR AIAQGSSERN ISAVIAAADV KKAINVLHED FFETTYKQIN LFVAGTGNVG
     SKLLAQLKQQ QHYLQQNMRL QVRIVGMANS KKMVFSDEGI DLDNWREHLQ QGEASDLGKF
     VETIRSKNLR NSVFVDVTAN EHVAQVYDQL LAKSISVVAC NKVACSSAYQ YYKKLKDLAR
     EYNAFFLFET NVGAGLPVIG TLNDLMRSGD VVTRIEAVLS GTLNFVFNNY DGTRSFAEVV
     KQAQDEGYTE PDPRLDLSGT DVMRKIMILA REAGEHLEME TISNNSFMPA SCMVGSVDDF
     YREMEKQETH FREIYQQAAA AGKKLKFVAK YEGGKASVGL QHVDSQSDFY HLYGKDNVVL
     FYTNRYPDQP LVVKGAGAGA EVTASGVFAD IIRAAH
//
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