ID A0A1C6RN87_9ACTN Unreviewed; 314 AA.
AC A0A1C6RN87;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Homoserine kinase {ECO:0000256|ARBA:ARBA00017858, 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|ARBA:ARBA00012078, ECO:0000256|HAMAP-Rule:MF_00384};
GN Name=thrB {ECO:0000256|HAMAP-Rule:MF_00384};
GN ORFNames=GA0070616_1560 {ECO:0000313|EMBL:SCL18657.1};
OS Micromonospora nigra.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=145857 {ECO:0000313|EMBL:SCL18657.1, ECO:0000313|Proteomes:UP000199699};
RN [1] {ECO:0000313|EMBL:SCL18657.1, ECO:0000313|Proteomes:UP000199699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43818 {ECO:0000313|EMBL:SCL18657.1,
RC ECO:0000313|Proteomes:UP000199699};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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|ARBA:ARBA00000528,
CC 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|ARBA:ARBA00005015,
CC 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|ARBA:ARBA00007370, ECO:0000256|HAMAP-
CC Rule:MF_00384}.
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DR EMBL; FMHT01000003; SCL18657.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C6RN87; -.
DR STRING; 145857.GA0070616_1560; -.
DR OrthoDB; 9769912at2; -.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000199699; 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; IPR006203; GHMP_knse_ATP-bd_CS.
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.
DR PROSITE; PS00627; GHMP_KINASES_ATP; 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:UP000199699};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697, ECO:0000256|HAMAP-
KW Rule:MF_00384};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00384}.
FT DOMAIN 87..150
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 229..270
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
FT BINDING 94..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00384"
SQ SEQUENCE 314 AA; 31573 MW; 6E33FA47F9F2E1F2 CRC64;
MSTTFAAGPV RVRVPATSAN LGPGFDALGL ALALHDDVVA EVTSGGVAVE VSGEGAGELP
ADDRHLVVRA MRETFDVLGG QPRGLAVECL NRIPQARGLG SSSAAIVAGV LLARALVSDG
PDRLDDAGVL RLAAGIEGHP DNVAPCLLGG FTLAWTEPTG ARAVSVPVAE GIMPTVFVPA
DRGLTATARA ALPATVPHGD AAFNAGRAAL LVHALTVDPS LLLPATVDRL HQVYRAAGMP
GTNALVDALR VAGVAAVVSG AGPTVLALTD LPEGFDAGTN WQVRQLPVDV SGAQVAGGRL
GHAERDPVAA GRKS
//
