ID A0A0K9XXZ9_9FLAO Unreviewed; 412 AA.
AC A0A0K9XXZ9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN ORFNames=AC804_08235 {ECO:0000313|EMBL:KNB61357.1};
OS Chryseobacterium sp. Hurlbut01.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1681828 {ECO:0000313|EMBL:KNB61357.1, ECO:0000313|Proteomes:UP000036769};
RN [1] {ECO:0000313|Proteomes:UP000036769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hurlbut01 {ECO:0000313|Proteomes:UP000036769};
RA Couger M.B., Youseff N., Elshahed M., French D., Hoff W.;
RT "Draft Genome Sequence of the Environmental Isolate Chryseobacterium sp.
RT Hurlbut 01.";
RL Submitted (JUL-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 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|RuleBase:RU004249}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 1/5. {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:KNB61357.1}.
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DR EMBL; LGIP01000019; KNB61357.1; -; Genomic_DNA.
DR RefSeq; WP_050378655.1; NZ_LGIP01000019.1.
DR AlphaFoldDB; A0A0K9XXZ9; -.
DR PATRIC; fig|1681828.3.peg.782; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000036769; 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 Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR Gene3D; 1.20.120.1320; Aspartokinase, catalytic domain; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR005260; Asp_kin_monofn.
DR InterPro; IPR001341; Asp_kinase.
DR InterPro; IPR042199; AsparK_Bifunc_asparK/hSer_DH.
DR NCBIfam; TIGR00657; asp_kinases; 1.
DR PANTHER; PTHR21499; ASPARTATE KINASE; 1.
DR PANTHER; PTHR21499:SF59; ASPARTOKINASE; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR PIRSF; PIRSF000726; Asp_kin; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004249};
KW ATP-binding {ECO:0000256|PIRSR:PIRSR000726-1};
KW Kinase {ECO:0000256|RuleBase:RU003448, ECO:0000313|EMBL:KNB61357.1};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000726-1};
KW Transferase {ECO:0000256|RuleBase:RU003448}.
FT DOMAIN 3..274
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
FT BINDING 5..8
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT BINDING 228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
SQ SEQUENCE 412 AA; 47165 MW; D3E37624241F5649 CRC64;
MKIFKFGGAS VKDAESVKNV SMVLKSQGFE KCLLVISAMG KTTNDLEKVV ELYFKKDDYQ
TEIEKIKQKH IEIAKGLFQN NHLVFDEINL FFDDIVSFLR RNKSPNYNFV YDQVVSCGEM
ISTKIVSEYL NDIHFTNQWL DARDYIKTDD SYRDGVVNWQ KTEEFIATLN PAICYVTQGF
IGSDDNNFTV TLGREGSDYS AAIFAYCLNA EAMTIWKDVP GVMTGDPRKF KDVSLLSNIS
YEEAIEMAYY GASIIHPKTL QPLQQKNIPF YVKSFVDPTK DGTKVGASEK NQHEESYILK
ENQTLLKIST RDFSFIAEDH MSLVFGYLSK YKIKVSLMQN SAISLALCLE DKFLKIDELN
NELQKVFKTD VIKNVSLFTV RNAKMENIGK FYQEKSVLLE QIAKNTLQMV TQ
//
