ID A0A285NY04_9AQUI Unreviewed; 408 AA.
AC A0A285NY04;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN ORFNames=SAMN06265353_1036 {ECO:0000313|EMBL:SNZ14329.1};
OS Hydrogenobacter hydrogenophilus.
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae;
OC Hydrogenobacter.
OX NCBI_TaxID=35835 {ECO:0000313|EMBL:SNZ14329.1, ECO:0000313|Proteomes:UP000218627};
RN [1] {ECO:0000313|EMBL:SNZ14329.1, ECO:0000313|Proteomes:UP000218627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2913 {ECO:0000313|EMBL:SNZ14329.1,
RC ECO:0000313|Proteomes:UP000218627};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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|ARBA:ARBA00004986, ECO:0000256|RuleBase:RU004249}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 1/5. {ECO:0000256|ARBA:ARBA00005139,
CC ECO:0000256|RuleBase:RU004249}.
CC -!- SIMILARITY: Belongs to the aspartokinase family.
CC {ECO:0000256|ARBA:ARBA00010122, ECO:0000256|RuleBase:RU003448}.
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DR EMBL; OBEN01000005; SNZ14329.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285NY04; -.
DR OrthoDB; 9799110at2; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000218627; 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: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; cd04261; AAK_AKii-LysC-BS; 1.
DR CDD; cd04923; ACT_AK-LysC-DapG-like_2; 1.
DR CDD; cd04913; ACT_AKii-LysC-BS-like_1; 1.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 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; IPR041740; AKii-LysC-BS.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR005260; Asp_kin_monofn.
DR InterPro; IPR001341; Asp_kinase.
DR InterPro; IPR018042; Aspartate_kinase_CS.
DR InterPro; IPR027795; CASTOR_ACT_dom.
DR NCBIfam; TIGR00656; asp_kin_monofn; 1.
DR NCBIfam; TIGR00657; asp_kinases; 1.
DR PANTHER; PTHR21499; ASPARTATE KINASE; 1.
DR PANTHER; PTHR21499:SF3; ASPARTOKINASE; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF01842; ACT; 1.
DR Pfam; PF13840; ACT_7; 1.
DR PIRSF; PIRSF000726; Asp_kin; 2.
DR SUPFAM; SSF55021; ACT-like; 2.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR PROSITE; PS51671; ACT; 2.
DR PROSITE; PS00324; ASPARTOKINASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU004249};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000726-
KW 1}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003448};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000726-1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003448}.
FT DOMAIN 262..336
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT DOMAIN 342..408
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT BINDING 6..9
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT BINDING 171..172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT BINDING 182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT BINDING 207..208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
SQ SEQUENCE 408 AA; 44754 MW; 4457AF290C43B59C CRC64;
MNLVVKFGGT SVGSLERIES AAEKVIQKVK QGYKVVVVSS AMAGETDRLI NLAKQIDPFP
PERELDMLIS TGEQQAIALF AITLNKMGYP AKSLCGWQVP IITDGVHTKA RVVKVGVQRI
KNLLNEGYIP VVAGFQGVTE DWEITTLGRG GSDLSAVVLA HALGADCEIY TDVEGVFTAD
PRIVPNAKKI SRISYEEMLE MASLGAKVMQ ARSIEFAMKY NVRIHVRSSF SDNDGTWILP
EEEVMEKVAV RAITLDTKES RITVVRVPDK PGIAYSIFKA LGDAHIVVDM IVQNVSHQGY
TDMSFTVNKT DAKIAEDIVR KVASEIGAQE VVRDDNVAKI SVVGIGMKSS YGTAAKMFEV
LYRNNINIMA ISTSEIKISC LIDSKYGELA LRELHSAFIE EDQDVVKY
//
