KHSE_YERPN
ID KHSE_YERPN Reviewed; 309 AA.
AC Q1CMW6; C4GNN4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Homoserine kinase {ECO:0000255|HAMAP-Rule:MF_00384};
DE Short=HK {ECO:0000255|HAMAP-Rule:MF_00384};
DE Short=HSK {ECO:0000255|HAMAP-Rule:MF_00384};
DE EC=2.7.1.39 {ECO:0000255|HAMAP-Rule:MF_00384};
GN Name=thrB {ECO:0000255|HAMAP-Rule:MF_00384}; OrderedLocusNames=YPN_0332;
GN ORFNames=YP516_0338;
OS Yersinia pestis bv. Antiqua (strain Nepal516).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=377628;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nepal516;
RX PubMed=16740952; DOI=10.1128/jb.00124-06;
RA Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nepal516;
RA Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L.,
RA Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R.,
RA Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.;
RT "Yersinia pestis Nepal516A whole genome shotgun sequencing project.";
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of L-homoserine
CC to L-homoserine phosphate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00384};
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00384}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00384}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00384}.
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DR EMBL; CP000305; ABG16664.1; -; Genomic_DNA.
DR EMBL; ACNQ01000006; EEO78116.1; -; Genomic_DNA.
DR RefSeq; WP_002209238.1; NZ_ACNQ01000006.1.
DR PDB; 4RPF; X-ray; 2.30 A; A/B/C=1-309.
DR PDBsum; 4RPF; -.
DR AlphaFoldDB; Q1CMW6; -.
DR SMR; Q1CMW6; -.
DR EnsemblBacteria; ABG16664; ABG16664; YPN_0332.
DR GeneID; 66842976; -.
DR KEGG; ypn:YPN_0332; -.
DR HOGENOM; CLU_041243_1_1_6; -.
DR OMA; CANRIPH; -.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000008936; 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; -; 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; ATP-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Threonine biosynthesis; Transferase.
FT CHAIN 1..309
FT /note="Homoserine kinase"
FT /id="PRO_1000049198"
FT BINDING 91..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00384"
FT STRAND 1..12
FT /evidence="ECO:0007829|PDB:4RPF"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:4RPF"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:4RPF"
FT STRAND 20..26
FT /evidence="ECO:0007829|PDB:4RPF"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:4RPF"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:4RPF"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:4RPF"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:4RPF"
FT HELIX 64..76
FT /evidence="ECO:0007829|PDB:4RPF"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:4RPF"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:4RPF"
FT HELIX 98..113
FT /evidence="ECO:0007829|PDB:4RPF"
FT HELIX 120..135
FT /evidence="ECO:0007829|PDB:4RPF"
FT HELIX 143..148
FT /evidence="ECO:0007829|PDB:4RPF"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:4RPF"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:4RPF"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:4RPF"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:4RPF"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:4RPF"
FT HELIX 197..215
FT /evidence="ECO:0007829|PDB:4RPF"
FT HELIX 219..225
FT /evidence="ECO:0007829|PDB:4RPF"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:4RPF"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:4RPF"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:4RPF"
FT HELIX 242..252
FT /evidence="ECO:0007829|PDB:4RPF"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:4RPF"
FT STRAND 266..272
FT /evidence="ECO:0007829|PDB:4RPF"
FT HELIX 273..286
FT /evidence="ECO:0007829|PDB:4RPF"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:4RPF"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:4RPF"
SQ SEQUENCE 309 AA; 33231 MW; 175F39BEB5A7B416 CRC64;
MVKIYAPASI GNVSVGFDVL GAAVSPIDGT LLGDCVSVTA AERFSLHNEG RFVSKLPDDP
KQNIVYQCWE RFCQEMGKEI PVAMVLEKNM PIGSGLGSSA CSVVAGLMAM NEFCGQPLDK
VTLLGMMGEL EGRVSGSIHF DNVAPCYLGG MQLILEQEGY ISQDVPGFSD WLWVMAYPGI
KVSTAEARAI LPAQYRRQDC ITHGRNLAGF IHACHTQQPD LAAKMMKDVI AEPYRTQLLP
GFAAARQAAQ DIGALACGIS GSGPTLFAVC NDQATAQRMA GWLQNHYLQN DEGFVHICRL
DTAGARLLG
