ID A0A1E5E153_9VIBR Unreviewed; 473 AA.
AC A0A1E5E153;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=aspartate kinase {ECO:0000256|ARBA:ARBA00013059};
DE EC=2.7.2.4 {ECO:0000256|ARBA:ARBA00013059};
GN ORFNames=A1QC_10260 {ECO:0000313|EMBL:OEF24297.1};
OS Vibrio rumoiensis 1S-45.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1188252 {ECO:0000313|EMBL:OEF24297.1, ECO:0000313|Proteomes:UP000094070};
RN [1] {ECO:0000313|EMBL:OEF24297.1, ECO:0000313|Proteomes:UP000094070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1S-45 {ECO:0000313|EMBL:OEF24297.1,
RC ECO:0000313|Proteomes:UP000094070};
RX PubMed=22955834; DOI=10.1126/science.1219385;
RA Cordero O.X., Wildschutte H., Kirkup B., Proehl S., Ngo L., Hussain F.,
RA Le Roux F., Mincer T., Polz M.F.;
RT "Ecological populations of bacteria act as socially cohesive units of
RT antibiotic production and resistance.";
RL Science 337:1228-1231(2012).
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 -!- SIMILARITY: Belongs to the aspartokinase family.
CC {ECO:0000256|ARBA:ARBA00010122}.
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:OEF24297.1}.
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DR EMBL; AJYK02000078; OEF24297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E5E153; -.
DR STRING; 1188252.A1QC_10260; -.
DR eggNOG; COG0527; Bacteria.
DR OrthoDB; 9799110at2; -.
DR Proteomes; UP000094070; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04915; ACT_AK-Ectoine_2; 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; IPR001048; Asp/Glu/Uridylate_kinase.
DR PANTHER; PTHR21499; ASPARTATE KINASE; 1.
DR PANTHER; PTHR21499:SF3; ASPARTOKINASE; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:OEF24297.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094070};
KW Transferase {ECO:0000313|EMBL:OEF24297.1}.
FT DOMAIN 20..285
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
SQ SEQUENCE 473 AA; 52617 MW; 311BA32C72FEA360 CRC64;
MSAFDAVLDN ILLRPQNPYN RMFVVSAYGG ITDALLECKR TGKAGIYRLV ENRDDAWTDA
IEVLEQRMLL INENMFADPI SRRRADNFIK DRIAQATNCI NNIMETCQYG QFSMQHYLPQ
IREFLSSIGE AHSAYNTCLK LKTLGINSTF VDLSGWDLDQ KNLGSGDLDS IIEQALMNID
VTKELPIVTG YVYCAEGLMK TYDRGYSEMT FSRLAVLSKA KQAVIHKEYH LSTADPRIVG
PEKVRPMGQT NYDVADQLAN LGMEAIHPNA ASGLRRSEIE LVIKNTFEPE HKGTLISHAF
DPHSYAGNSD KVEIIAGRNK VFALHIFDQA MVGQADNVSY ELMEIINDEH VQLVGKEMNA
NSITYYLSGN SKSKNKVLSR AEKAFPNAKI TGKMVALISV IGASIDTNKA LSHGMIALMN
QDITPKAAHS SMRNVDVQFV VDDENYEAAI CTLHEAFIDG VQVKSKVKEE QAA
//
