ID A0A1X3PAC5_9MICC Unreviewed; 347 AA.
AC A0A1X3PAC5;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=BCY76_003980 {ECO:0000313|EMBL:OSM44196.1};
OS Nesterenkonia sp. PF2B19.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Nesterenkonia.
OX NCBI_TaxID=1881858 {ECO:0000313|EMBL:OSM44196.1, ECO:0000313|Proteomes:UP000175621};
RN [1] {ECO:0000313|EMBL:OSM44196.1, ECO:0000313|Proteomes:UP000175621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF2B19 {ECO:0000313|EMBL:OSM44196.1,
RC ECO:0000313|Proteomes:UP000175621};
RX PubMed=28408669;
RA Singh P., Kapse N., Roy U., Singh S.M., Dhakephalkar P.K.;
RT "Draft Genome Sequence of Permafrost Bacterium Nesterenkonia sp. Strain
RT PF2B19, Revealing a Cold Adaptation Strategy and Diverse Biotechnological
RT Potential.";
RL Genome Announc. 5:e00133-17(2017).
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}.
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:OSM44196.1}.
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DR EMBL; MDSS02000008; OSM44196.1; -; Genomic_DNA.
DR RefSeq; WP_070162160.1; NZ_MDSS02000008.1.
DR AlphaFoldDB; A0A1X3PAC5; -.
DR STRING; 1881858.BCY76_003980; -.
DR OrthoDB; 9769912at2; -.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000175621; 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};
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 125..185
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 255..317
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
FT REGION 16..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 132..142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00384"
SQ SEQUENCE 347 AA; 36274 MW; 6B14060164F11D1D CRC64;
MGITLGQGFG AEEALTGESR SAQHPGSPAA PLTAPLTAPR SFRLRVPATS ANLGPGYDCM
GLALDLHDII DVVATPRRDG DRPQVTVSVE GEGAATLPRD ATHLVVSLIE RIMARHGVGM
PDLEVRAHNH IPHSRGLGSS AAAVASAVII ADELLPDGLT DEEKLQIGSR VEGHPDNYVP
ALRGGVALSW QEGDRFHTVP LIPHEELRTV LAVPDVEQST AEARGVLPEV VLHADAAANS
ARTGLLVHAL TSAPELLLAA TCDRLHQEQR RAAFAPSMAL VDSLREAGHA AVISGAGPSV
LVLAAGDSAA RAARSHIADH AARTDDMWTP AILPISRAGA TVEEYPR
//
