ID A0A0D8CEZ4_9PROT Unreviewed; 501 AA.
AC A0A0D8CEZ4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=aspartate kinase {ECO:0000256|ARBA:ARBA00013059};
DE EC=2.7.2.4 {ECO:0000256|ARBA:ARBA00013059};
GN ORFNames=UF64_13575 {ECO:0000313|EMBL:KJE34734.1};
OS Thalassospira sp. HJ.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Thalassospiraceae; Thalassospira.
OX NCBI_TaxID=1616823 {ECO:0000313|EMBL:KJE34734.1, ECO:0000313|Proteomes:UP000032356};
RN [1] {ECO:0000313|EMBL:KJE34734.1, ECO:0000313|Proteomes:UP000032356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HJ {ECO:0000313|EMBL:KJE34734.1,
RC ECO:0000313|Proteomes:UP000032356};
RA Kiseleva L., Garushyants S.K., Goryanin I.;
RT "Complete genome of Thalassospira sp. strain HJ.";
RL Submitted (FEB-2015) 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 -!- 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:KJE34734.1}.
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DR EMBL; JYII01000015; KJE34734.1; -; Genomic_DNA.
DR RefSeq; WP_044829149.1; NZ_JYII01000015.1.
DR AlphaFoldDB; A0A0D8CEZ4; -.
DR STRING; 1616823.UF64_13575; -.
DR PATRIC; fig|1616823.3.peg.4009; -.
DR OrthoDB; 9799110at2; -.
DR Proteomes; UP000032356; Unassembled WGS sequence.
DR GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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:KJE34734.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032356};
KW Transferase {ECO:0000313|EMBL:KJE34734.1}.
FT DOMAIN 14..307
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
FT REGION 476..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 501 AA; 54888 MW; 3AFC6C4A3C54D814 CRC64;
MLSAQKNKDA GHSVHKIGGT SMTQVDAVMD NILVGNRKED ELYNRVFVVS AYGGFTDLLL
ENKKTGEAGV YQLYAGSETD WAWGDALTKV SEKMCAINEE IFGDAPELKL ANAFVQERIE
GTRSCLMDLH RLCSFGHFKL EKHLLTVREM LSAIGEAHSA HNTMLLLRAK GVNAVFADLS
GWREPEASTL DGRINKVFED IDLSSQLAIA TGYAQCSEGL MSIYGRGYSE VTFSRIACLT
QAREAIIHKE FHLSSADPRI VGEDAVRPIG RTSYDVADQL SNMGMEAIHP RAAKGLRQND
IPLRIANTFE PEHPGTVIDD HWEPENSRVE IVTGVPTAFE IEVFNQDMVG VPGGEEALLN
VLKRYKVPTV TKNLNANTIT HYVAAPLKQI RRCVDEIEAN QPEATVQTRK VAIVSVIGAN
IEQPGLFARA VSILDDAGVE LVASHYPSRR VDLQFVVAEG DFNKAIVALH RGLVEGKKES
GASSKKTNDD SATTQEKLKA A
//
