KHSE_SERMA
ID KHSE_SERMA Reviewed; 309 AA.
AC P27722;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Homoserine kinase;
DE Short=HK;
DE Short=HSK;
DE EC=2.7.1.39;
GN Name=thrB;
OS Serratia marcescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sr41;
RX PubMed=8423151; DOI=10.1128/jb.175.3.785-794.1993;
RA Omori K., Suzuki S., Komatsubara S.;
RT "Nucleotide sequence of the Serratia marcescens threonine operon and
RT analysis of the threonine operon mutations which alter feedback inhibition
RT of both aspartokinase I and homoserine dehydrogenase I.";
RL J. Bacteriol. 175:785-794(1993).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of L-homoserine
CC to L-homoserine phosphate. {ECO:0000250}.
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;
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 4/5.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase
CC subfamily. {ECO:0000305}.
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DR EMBL; D10387; BAA38482.1; -; Genomic_DNA.
DR EMBL; X60821; CAA43213.1; -; Genomic_DNA.
DR PIR; C47057; C47057.
DR RefSeq; WP_004932993.1; NZ_WUUW01000008.1.
DR AlphaFoldDB; P27722; -.
DR SMR; P27722; -.
DR STRING; 273526.SMDB11_0002; -.
DR GeneID; 64310061; -.
DR GeneID; 66716345; -.
DR OrthoDB; 610857at2; -.
DR UniPathway; UPA00050; UER00064.
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; -; 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_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PIRSF; PIRSF000676; Homoser_kin; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
DR TIGRFAMs; TIGR00191; thrB; 1.
DR PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; ATP-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Threonine biosynthesis; Transferase.
FT CHAIN 1..309
FT /note="Homoserine kinase"
FT /id="PRO_0000156602"
FT BINDING 91..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 309 AA; 33387 MW; 7F491BDC1F4B2A49 CRC64;
MVKVYAPASI GNVSVGFDVL GAAVSPIDGT LLGDCVSVEA AETFSLQNAG RFVSKLPAEP
KENIVYQCWE RFCQEIGREV PVAMRLEKNM PIGSGLGSSA CSVVAGLMAM NEFCDRPLDK
TTLLGLMGEL EGRISGSVHY DNVAPCYLGG LQLMLEEEGI ISQEVPCFDD WLWVMAYPGI
KVSTAEARAI LPAQYRRQDC ISHGRYLAGF IHACHTRQPQ LAAKLMQDVI AEPYRTRLLP
GFAEARKAAQ EIGALACGIS GSGPTLFAVC NDGATAQRMA AWLQQHYLQN DEGFVHICRL
DTAGARLLG
