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Entry: A0A3N2NQJ5_9BACT
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ID   A0A3N2NQJ5_9BACT        Unreviewed;       456 AA.
AC   A0A3N2NQJ5;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE            EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN   ORFNames=EEL53_02445 {ECO:0000313|EMBL:ROT24180.1};
OS   Muribaculaceae bacterium Isolate-114 (HZI).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae.
OX   NCBI_TaxID=2486475 {ECO:0000313|EMBL:ROT24180.1, ECO:0000313|Proteomes:UP000273368};
RN   [1] {ECO:0000313|EMBL:ROT24180.1, ECO:0000313|Proteomes:UP000273368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate-114 (HZI) {ECO:0000313|Proteomes:UP000273368};
RA   Clavel T., Strowig T.;
RT   "Sequence and cultivation study of Muribaculaceae reveals novel species,
RT   host preference, and functional potential of this yet undescribed family.";
RL   Submitted (NOV-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         ECO:0000256|RuleBase:RU003448};
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|RuleBase:RU004249}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-homoserine from L-aspartate: step 1/3.
CC       {ECO:0000256|RuleBase:RU004249}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 1/5. {ECO:0000256|RuleBase:RU004249}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the aspartokinase family.
CC       {ECO:0000256|RuleBase:RU003448}.
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:ROT24180.1}.
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DR   EMBL; RIBN01000002; ROT24180.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N2NQJ5; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000273368; 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: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   Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR   Gene3D; 1.20.120.1320; Aspartokinase, catalytic 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; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR005260; Asp_kin_monofn.
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   NCBIfam; TIGR00657; asp_kinases; 1.
DR   PANTHER; PTHR43070; -; 1.
DR   PANTHER; PTHR43070:SF3; HOMOSERINE DEHYDROGENASE; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   PIRSF; PIRSF000726; Asp_kin; 1.
DR   SUPFAM; SSF55021; ACT-like; 2.
DR   SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR   PROSITE; PS00324; ASPARTOKINASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004249};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000726-
KW   1}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003448};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR000726-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000273368};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003448}.
FT   DOMAIN          1..279
FT                   /note="Aspartate/glutamate/uridylate kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00696"
FT   COILED          81..108
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         6..9
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT   BINDING         43
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT   BINDING         124
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT   BINDING         222..223
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT   BINDING         233
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT   BINDING         258..259
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
SQ   SEQUENCE   456 AA;  49163 MW;  07CEBE3F2B330CDB CRC64;
     MLKVLKFGGT SVGTVESLRN VKAIVEGLEI PAIVVVSALG GLTDRLIATA KSASEGKEDY
     TDEMKVIRKR HYDIISALVP EERKAEVLAK VDELLDQLEE RYKGLTLIRL LPERTLAEVV
     SFGERMSSVI VAAMLENASH HNSLDFIKTE KWFNRNIADR GLTEKLIKEE FALPLERHAV
     AGGFISTDRN TGEITNLGRG GSDYTAALIA AALDADLLEI WTDVDGFMTS DPRIIKEAAI
     IPSMSFVESM ELCSFGAKVI YPPTIYPVFH KNIPIKILNT FNPTAPGTLI SDNAPGKGKA
     RGVSSLNSTS MISMSGPLAS NVAEINSRAY NAMARNGISV FLVAQPSEEK TFSIAMPQSD
     GEKALEQLKL EFSPEIQSGE LLSIEKTDDL SVIAVVGEGI KTAKGLGARI VETLRGADVD
     VKAISEGASD TTVAVVLESA KVREGLNLIH SLCFVS
//
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