ID C0BMV8_9BACT Unreviewed; 306 AA.
AC C0BMV8;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 77.
DE RecName: Full=Homoserine kinase {ECO:0000256|HAMAP-Rule:MF_00384};
DE Short=HK {ECO:0000256|HAMAP-Rule:MF_00384};
DE Short=HSK {ECO:0000256|HAMAP-Rule:MF_00384};
DE EC=2.7.1.39 {ECO:0000256|HAMAP-Rule:MF_00384};
GN Name=thrB {ECO:0000256|HAMAP-Rule:MF_00384};
GN ORFNames=Flav3CDRAFT_0449 {ECO:0000313|EMBL:EEG43055.1};
OS Flavobacteria bacterium MS024-3C.
OC Bacteria; Bacteroidota; Flavobacteriia.
OX NCBI_TaxID=487797 {ECO:0000313|EMBL:EEG43055.1, ECO:0000313|Proteomes:UP000003631};
RN [1] {ECO:0000313|EMBL:EEG43055.1, ECO:0000313|Proteomes:UP000003631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS024-3C {ECO:0000313|EMBL:EEG43055.1,
RC ECO:0000313|Proteomes:UP000003631};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Woyke T., Xie G., Copeland A., Gonzalez J., Han C., Kiss H., Saw J.,
RA Senin P., Chatterji S., Cheng J.-F., Eisen J.A., Sieracki M.E.,
RA Stepanauskas R.;
RT "Assembling the metagenome, one cell at a time.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of L-homoserine
CC to L-homoserine phosphate. {ECO:0000256|HAMAP-Rule:MF_00384}.
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_00384};
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 4/5. {ECO:0000256|HAMAP-Rule:MF_00384}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00384}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00384}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00384}.
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:EEG43055.1}.
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DR EMBL; ABVW01000004; EEG43055.1; -; Genomic_DNA.
DR AlphaFoldDB; C0BMV8; -.
DR STRING; 487797.Flav3CDRAFT_0449; -.
DR OrthoDB; 9769912at2; -.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000003631; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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 Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; GHMP kinase, C-terminal domain; 1.
DR HAMAP; MF_00384; Homoser_kinase; 1.
DR InterPro; IPR013750; GHMP_kinase_C_dom.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR000870; Homoserine_kinase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00191; thrB; 1.
DR PANTHER; PTHR20861:SF1; HOMOSERINE KINASE; 1.
DR PANTHER; PTHR20861; HOMOSERINE/4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL KINASE; 1.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PIRSF; PIRSF000676; Homoser_kin; 1.
DR PRINTS; PR00958; HOMSERKINASE.
DR SUPFAM; SSF55060; GHMP Kinase, C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00384};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00384}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00384};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00384};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00384}; Reference proteome {ECO:0000313|Proteomes:UP000003631};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697, ECO:0000256|HAMAP-
KW Rule:MF_00384}; Transferase {ECO:0000256|HAMAP-Rule:MF_00384}.
FT DOMAIN 80..147
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 208..284
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
SQ SEQUENCE 306 AA; 31869 MW; 1339E4692BA7E45A CRC64;
MKSIRVFCPG TIANVSCGFD VLGLSLAGVG EYMTVTQTPT KGITISEITG QDLPLETAKN
VAGVAGLALL EALGSEAGFD IKIEKKIKAG SGIGSSAASS AGAVWAINHL LGNPYTTIEL
IPFAMEGERL ASGVAHADNV APALLGGFTL VRSTDPLDVV SLPSPRELYA TVIHPQIEIK
TADSRRILKS SLSLKDAITQ WGNVGGLVAG LYREDYELIG RSLQDVVIEP VRSILIPGFD
EIKAAALNAG AMGCGISGSG PSVFALSKGA DKAHEVAQQL KEVYTPMGIP FDIHISNINE
KGVYPA
//
