ID A0A385C585_9GAMM Unreviewed; 426 AA.
AC A0A385C585;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN ORFNames=BEN71_08280 {ECO:0000313|EMBL:AXQ22062.1}, CDG68_14145
GN {ECO:0000313|EMBL:AYO54720.1}, EXU28_10145
GN {ECO:0000313|EMBL:RZG46125.1};
OS Acinetobacter wuhouensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1879050 {ECO:0000313|EMBL:AXQ22062.1, ECO:0000313|Proteomes:UP000257257};
RN [1] {ECO:0000313|EMBL:AXQ22062.1, ECO:0000313|Proteomes:UP000257257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCHA60 {ECO:0000313|EMBL:AXQ22062.1,
RC ECO:0000313|Proteomes:UP000257257};
RX PubMed=30117799; DOI=10.1099/ijsem.0.002963;
RA Hu Y., Feng Y., Qin J., Radolfova-Krizova L., Maixnerova M., Zhang X.,
RA Nemec A., Zong Z.;
RT "Acinetobacter wuhouensis sp. nov., isolated from hospital sewage.";
RL Int. J. Syst. Evol. Microbiol. 68:3212-3216(2018).
RN [2] {ECO:0000313|EMBL:AYO54720.1, ECO:0000313|Proteomes:UP000279962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCHAW010062 {ECO:0000313|EMBL:AYO54720.1,
RC ECO:0000313|Proteomes:UP000279962};
RA Hu Y., Long H., Feng Y., Zong Z.;
RT "The complete genome of Acinetobacter wuhouensis strain WCHAW010062.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:RZG46125.1, ECO:0000313|Proteomes:UP000293863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCHAW060049 {ECO:0000313|EMBL:RZG46125.1,
RC ECO:0000313|Proteomes:UP000293863};
RA Qin J., Hu Y., Ye H., Wei L., Feng Y., Zong Z.;
RT "The Batch Genome Submission of Acinetobacter spp. strains.";
RL Submitted (FEB-2019) 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; CP031716; AXQ22062.1; -; Genomic_DNA.
DR EMBL; CP033133; AYO54720.1; -; Genomic_DNA.
DR EMBL; SGSQ01000014; RZG46125.1; -; Genomic_DNA.
DR RefSeq; WP_068974245.1; NZ_SGSR01000020.1.
DR AlphaFoldDB; A0A385C585; -.
DR STRING; 1879050.GCA_001696605_01570; -.
DR KEGG; awu:BEN71_08280; -.
DR OrthoDB; 9799110at2; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000257257; Chromosome.
DR Proteomes; UP000279962; Chromosome.
DR Proteomes; UP000293863; 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 277..351
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT DOMAIN 357..426
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 426 AA; 45803 MW; 1C0FE89D1440D947 CRC64;
MALIVQKYGG TSMGTPERIL NVARRVKRWH DHGHKVVVVV SAMSGETNRL LALAKAITET
PDPRELDQMV STGEQVTISM LAMALNSIGV AAKSLTGRQV GIKTDNSYTK ARIESIDTDV
MTGHLDAGRV IVVAGFQGFD AEGNTTTLGR GGSDTSGVAL AAALKADECQ IYTDVDGVYT
TDPRVAPKAK KVDRISFEEM LEMASLGSKV LQIRSVEFAG KYQVPLRVLS SFDNDDDGAF
DEEFKKNVGT LITTEAEDNM ENPIISGIAF NRDEAKLTIL GVPDEPGIAS KILSPIGAAN
VEVDMIIQNV EEDGTTDFTF TVNRGELKKA KAILEETARA IGAREVATRD DIVKVSIVGV
GMRSHAGVAS KMFTALADEG INILMISTSE IKISVIIEEN YLELAVRTLH TAFGLDREHG
ESSVRA
//
