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Database: UniProt
Entry: A0A081G0P0_9GAMM
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ID   A0A081G0P0_9GAMM        Unreviewed;       411 AA.
AC   A0A081G0P0;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE            EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN   ORFNames=ADIMK_1591 {ECO:0000313|EMBL:KEA64345.1};
OS   Marinobacterium lacunae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinobacterium.
OX   NCBI_TaxID=1232683 {ECO:0000313|EMBL:KEA64345.1, ECO:0000313|Proteomes:UP000028252};
RN   [1] {ECO:0000313|EMBL:KEA64345.1, ECO:0000313|Proteomes:UP000028252}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK27 {ECO:0000313|EMBL:KEA64345.1,
RC   ECO:0000313|Proteomes:UP000028252};
RA   Singh A., Pinnaka A.K.;
RT   "Marinobacterium kochiensis sp. nov., isolated from sediment sample
RT   collected from Kochi backwaters in Kerala, India.";
RL   Submitted (APR-2014) 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}.
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:KEA64345.1}.
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DR   EMBL; JMQN01000018; KEA64345.1; -; Genomic_DNA.
DR   RefSeq; WP_036185948.1; NZ_JMQN01000018.1.
DR   AlphaFoldDB; A0A081G0P0; -.
DR   STRING; 1232683.ADIMK_1591; -.
DR   PATRIC; fig|1232683.4.peg.1571; -.
DR   eggNOG; COG0527; Bacteria.
DR   OrthoDB; 9799110at2; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000028252; 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; 1.
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:UP000028252};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003448}.
FT   DOMAIN          265..348
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   411 AA;  44330 MW;  BFA682281113B0D5 CRC64;
     MALYVQKYGG TSVGSVERIE AVAEKVKGFR ERGDDIVVVV SAMSGETNRL IGLANEIQEH
     PDKREMDVLV STGEQVTIAL LAMALKKRGV DARSYTGGQV RILTDSAHTK ARIQDIETTR
     MRADLEAGRV VIVAGFQGVD DHGNITTLGR GGSDTTGVAL AAALKADECQ IYTDVDGVYT
     TDPRVVAGAQ RLDKITFEEM LEMASLGSKV LQIRSVEFAG KYHVPLRVLS SFQDGPGTLI
     TIEDDETVEK PIISGIAFNR DEAKLTVMGV PDIPGVASRI LGPISRENIE VDMIVQNVSA
     DQTTDFTFTV HRNDFERAQN ILEQVVTELG ARGCSGNSKI AKVSIVGVGM RSHAGVASKM
     FDALAAENIN IQMISTSEIK VSVVIAEKYM ELAVRALHTA FNLDKGETVC E
//
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