ID F0Q8E2_PARA1 Unreviewed; 324 AA. AC F0Q8E2; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAR-2024, entry version 65. DE RecName: Full=Homoserine kinase {ECO:0000256|HAMAP-Rule:MF_00301}; DE Short=HK {ECO:0000256|HAMAP-Rule:MF_00301}; DE Short=HSK {ECO:0000256|HAMAP-Rule:MF_00301}; DE EC=2.7.1.39 {ECO:0000256|HAMAP-Rule:MF_00301}; GN Name=thrB {ECO:0000256|HAMAP-Rule:MF_00301}; GN OrderedLocusNames=Acav_3238 {ECO:0000313|EMBL:ADX47140.1}; OS Paracidovorax avenae (strain ATCC 19860 / DSM 7227 / CCUG 15838 / JCM 20985 OS / LMG 2117 / NCPPB 1011) (Acidovorax avenae). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Paracidovorax. OX NCBI_TaxID=643561 {ECO:0000313|EMBL:ADX47140.1, ECO:0000313|Proteomes:UP000002482}; RN [1] {ECO:0000313|Proteomes:UP000002482} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19860 / DSM 7227 / CCUG 15838 / JCM 20985 / LMG 2117 / RC NCPPB 1011 {ECO:0000313|Proteomes:UP000002482}; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Gordon S., Woyke T.; RT "Complete sequence of Acidovorax avenae subsp. avenae ATCC 19860."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine; CC Xref=Rhea:RHEA:13985, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:57476, ChEBI:CHEBI:57590, ChEBI:CHEBI:456216; CC EC=2.7.1.39; Evidence={ECO:0000256|HAMAP-Rule:MF_00301}; CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine CC from L-aspartate: step 4/5. {ECO:0000256|HAMAP-Rule:MF_00301}. CC -!- SIMILARITY: Belongs to the pseudomonas-type ThrB family. CC {ECO:0000256|HAMAP-Rule:MF_00301}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP002521; ADX47140.1; -; Genomic_DNA. DR RefSeq; WP_013595628.1; NC_015138.1. DR AlphaFoldDB; F0Q8E2; -. DR GeneID; 34238973; -. DR KEGG; aaa:Acav_3238; -. DR HOGENOM; CLU_053300_0_0_4; -. DR OrthoDB; 9777460at2; -. DR UniPathway; UPA00050; UER00064. DR Proteomes; UP000002482; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004413; F:homoserine kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd05153; HomoserineK_II; 1. DR Gene3D; 3.90.1200.10; -; 1. DR HAMAP; MF_00301; Homoser_kinase_2; 1. DR InterPro; IPR002575; Aminoglycoside_PTrfase. DR InterPro; IPR005280; Homoserine_kinase_II. DR InterPro; IPR011009; Kinase-like_dom_sf. DR NCBIfam; TIGR00938; thrB_alt; 1. DR PANTHER; PTHR21064:SF6; APH DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR21064; UNCHARACTERIZED; 1. DR Pfam; PF01636; APH; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_00301}; ATP-binding {ECO:0000256|HAMAP-Rule:MF_00301}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00301, ECO:0000313|EMBL:ADX47140.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00301}; KW Reference proteome {ECO:0000313|Proteomes:UP000002482}; KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697, ECO:0000256|HAMAP- KW Rule:MF_00301}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00301, ECO:0000313|EMBL:ADX47140.1}. FT DOMAIN 27..258 FT /note="Aminoglycoside phosphotransferase" FT /evidence="ECO:0000259|Pfam:PF01636" SQ SEQUENCE 324 AA; 36138 MW; 480027D2CBA07CF9 CRC64; MAVFTEVSKK EARDLLRRLQ LGTLESLRGI EGGIENTNYF LTSDQGEYVL TLFERLTAEQ LPFYLHLMKH LAQAGMPVPD PRGDRHGNIL HTVAGKPAAV VNKLPGRSQL APEPVHCAAV GGMLARMHLA GRDYERRQPN LRGLAWWNET VPVVLPHIGE SQRTLLRSEL AYQNHVAASA GYAALPRGPV HADLFRDNAM FDGEVLTGFF DFYFAGVDTW LFDLAVCLND WCIDWPTGLH APGRATAMLD AYQAVRPLSA DERALLPAML RAGALRFWIS RLWDFHLPRE ASLLTPHDPT HFERVLRGRI AQPLHVRAGG GFAE //