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Database: UniProt
Entry: A0A376BV71_9NEIS
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ID   A0A376BV71_9NEIS        Unreviewed;       406 AA.
AC   A0A376BV71;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE            EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN   Name=lysC {ECO:0000313|EMBL:SSY80809.1};
GN   ORFNames=NCTC10283_02370 {ECO:0000313|EMBL:SSY80809.1};
OS   Alysiella crassa.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Alysiella.
OX   NCBI_TaxID=153491 {ECO:0000313|EMBL:SSY80809.1, ECO:0000313|Proteomes:UP000254209};
RN   [1] {ECO:0000313|EMBL:SSY80809.1, ECO:0000313|Proteomes:UP000254209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC10283 {ECO:0000313|EMBL:SSY80809.1,
RC   ECO:0000313|Proteomes:UP000254209};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-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|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; UFSO01000003; SSY80809.1; -; Genomic_DNA.
DR   RefSeq; WP_034292452.1; NZ_UFSO01000003.1.
DR   AlphaFoldDB; A0A376BV71; -.
DR   STRING; 1120980.GCA_000745955_01078; -.
DR   OrthoDB; 9799110at2; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000254209; 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   Reference proteome {ECO:0000313|Proteomes:UP000254209};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003448}.
FT   DOMAIN          266..340
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   DOMAIN          346..406
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   BINDING         7..10
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT   BINDING         47
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT   BINDING         173..174
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT   BINDING         179
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT   BINDING         184
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT   BINDING         209..210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
SQ   SEQUENCE   406 AA;  43663 MW;  5786717BC9F93D2E CRC64;
     MALIVQKYGG TSVGSAERIK NVANRVKKAR DEGHDVVVVV SAMSGETNRL VALAHEMQEF
     PDPRELDVVL ATGEQVTIGL LAMALKNIGV DAKSYTGWQV AVKTDTAHTK ARIEEIDGDK
     MLADLKAGRV VIVAGFQGIS SEGDIATLGR GGSDTSAVAL AAALKADECQ IYTDVDGVYT
     TDPRVVPEAK RMDTITFEEM LELASLGSKV LQIRSVEFAG KYQVRLRVLS SLQEGGNGTL
     ITFEEDENME RAVVSGIAFD KNQARINVRG VPDKPGIAYQ ILGAVADANI EVDMIIQNVG
     NEGTTDFSFT VPRGDYKPTL ELLEQLKNTI GATEVSGDDA VCKVSIVGLG MRSHVGVASA
     MFRALAAESI NIQMISTSEI KVSVLIDEKY LELATRVLHK EFELDK
//
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