ID   A0A1V1UFP3_9RHOB        Unreviewed;       478 AA.
AC   A0A1V1UFP3;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=aspartate kinase {ECO:0000256|ARBA:ARBA00013059};
DE            EC=2.7.2.4 {ECO:0000256|ARBA:ARBA00013059};
GN   Name=thrA {ECO:0000313|EMBL:GAW34554.1};
GN   ORFNames=RA2_01604 {ECO:0000313|EMBL:GAW34554.1};
OS   Roseovarius sp. A-2.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=1570360 {ECO:0000313|EMBL:GAW34554.1, ECO:0000313|Proteomes:UP000191225};
RN   [1] {ECO:0000313|EMBL:GAW34554.1, ECO:0000313|Proteomes:UP000191225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A-2 {ECO:0000313|EMBL:GAW34554.1,
RC   ECO:0000313|Proteomes:UP000191225};
RA   Harada M., Ito K., Nakajima N., Yamamura S., Tomita M., Suzuki H.,
RA   Amachi S.;
RT   "Genome sequencing of bacteria contributing to the geochemical cycling of
RT   arsenic, bromine, and iodine.";
RL   Submitted (NOV-2016) 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:GAW34554.1}.
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DR   EMBL; BDIY01000004; GAW34554.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V1UFP3; -.
DR   STRING; 1570360.RA2_01604; -.
DR   OrthoDB; 9799110at2; -.
DR   Proteomes; UP000191225; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd04910; ACT_AK-Ectoine_1; 1.
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:GAW34554.1};
KW   Transferase {ECO:0000313|EMBL:GAW34554.1}.
FT   DOMAIN          7..301
FT                   /note="Aspartate/glutamate/uridylate kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00696"
SQ   SEQUENCE   478 AA;  52073 MW;  27026C5B7307634D CRC64;
     MTFPTHTVEK IGGTSMSRVN ELLDTLFIGG REGQRLYHRA FVVSAFGGIT NKLLEHKKSG
     TPGVYALFAN ADDDHGWLDA LTEVGTAMRA AHGEILEHPG DRSMADEFVR ERIEGARSCL
     FDLQRLCSYG HFRLSDHMLV IRELLSGLGE AHSAFVTTLL LQRAGVNARF IDLSGWRDET
     EHTLSERIAQ GLGDVDLATE MPIITGYAQC TEGLMREFDR GYSEVTFARI AAYTSATEAI
     IHKEFHLSSA DPKLVGEEAV RKLGHTNYDV ADQLSNLGME AIHPKAAKTL RQAEVSLRVT
     NAFDPGDPGT LIDDQPAKEA NVEIVTGLKV VALELFEQDM VGVKGYDAAI LEALKRHNVW
     IVSKTSNANT ITHYVHASLK VVRRVARDLE EQFTSATVSA RTLSLVSPIG RDLSGLKVLS
     RGLSALEEAG IEVIAAHQTP RGVDVQFVLS AADMEAGITA LHRALIEGTV AQVPKKAA
//