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
//