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Database: UniProt
Entry: B7GKL0_ANOFW
LinkDB: B7GKL0_ANOFW
Original site: B7GKL0_ANOFW 
ID   B7GKL0_ANOFW            Unreviewed;       304 AA.
AC   B7GKL0;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   24-JAN-2024, entry version 92.
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   ECO:0000313|EMBL:ACJ34769.1};
GN   OrderedLocusNames=Aflv_2412 {ECO:0000313|EMBL:ACJ34769.1};
OS   Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX   NCBI_TaxID=491915 {ECO:0000313|EMBL:ACJ34769.1, ECO:0000313|Proteomes:UP000000742};
RN   [1] {ECO:0000313|EMBL:ACJ34769.1, ECO:0000313|Proteomes:UP000000742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21510 / WK1 {ECO:0000313|Proteomes:UP000000742};
RX   PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA   Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA   Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA   Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT   "Encapsulated in silica: genome, proteome and physiology of the
RT   thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL   Genome Biol. 9:R161.1-R161.16(2008).
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; CP000922; ACJ34769.1; -; Genomic_DNA.
DR   RefSeq; WP_012575931.1; NC_011567.1.
DR   AlphaFoldDB; B7GKL0; -.
DR   STRING; 491915.Aflv_2412; -.
DR   GeneID; 7038685; -.
DR   KEGG; afl:Aflv_2412; -.
DR   PATRIC; fig|491915.6.peg.2485; -.
DR   eggNOG; COG0083; Bacteria.
DR   HOGENOM; CLU_041243_0_0_9; -.
DR   OMA; CANRIPH; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000000742; Chromosome.
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:UP000000742};
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          82..143
FT                   /note="GHMP kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00288"
FT   DOMAIN          204..277
FT                   /note="GHMP kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08544"
FT   BINDING         90..100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00384"
SQ   SEQUENCE   304 AA;  32643 MW;  0962A5C97D1057C3 CRC64;
     MNDGEMLKIV VPGSTANLGP GFDSIGLAVS LHLTLEVVRA ESWEFIPKTD EVKSIPTDES
     NLIYQVASKL ASKYGVTLPP CHVFVSSNIP FTRGLGSSAA AIVAAIELAN ELGCLCLSQE
     EKMRAASVYE GHPDNVGASL YGGLVIGSHL NERTHVVNIP HIPIDLIAVI PAYELETKKS
     RTVLPSAFTR AQAVEASAIS NVLVAALLTH NWSLVGEMMD ADVFHQPYRE SLVPELQHVR
     TVAKRNGAFG VALSGAGPTV LCFAERGQGE KVYHALKVAF PYSDVRMLSV EETGSCVYKM
     ALEK
//
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