KHSE_METJA
ID KHSE_METJA Reviewed; 296 AA.
AC Q58504;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Homoserine kinase;
DE Short=HK;
DE Short=HSK;
DE EC=2.7.1.39;
GN Name=thrB; OrderedLocusNames=MJ1104;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=11188689; DOI=10.1016/s0969-2126(00)00533-5;
RA Zhou T., Daugherty M., Grishin N.V., Osterman A.L., Zhang H.;
RT "Structure and mechanism of homoserine kinase: prototype for the GHMP
RT kinase superfamily.";
RL Structure 8:1247-1257(2000).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB99107.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L77117; AAB99107.1; ALT_INIT; Genomic_DNA.
DR PIR; G64437; G64437.
DR RefSeq; WP_064496725.1; NC_000909.1.
DR PDB; 1FWK; X-ray; 2.10 A; A/B/C/D=1-296.
DR PDB; 1FWL; X-ray; 2.25 A; A/B/C/D=1-296.
DR PDB; 1H72; X-ray; 1.80 A; C=1-296.
DR PDB; 1H73; X-ray; 2.00 A; A=1-296.
DR PDB; 1H74; X-ray; 1.90 A; A/B/C/D=1-296.
DR PDBsum; 1FWK; -.
DR PDBsum; 1FWL; -.
DR PDBsum; 1H72; -.
DR PDBsum; 1H73; -.
DR PDBsum; 1H74; -.
DR AlphaFoldDB; Q58504; -.
DR SMR; Q58504; -.
DR STRING; 243232.MJ_1104; -.
DR EnsemblBacteria; AAB99107; AAB99107; MJ_1104.
DR GeneID; 1452001; -.
DR KEGG; mja:MJ_1104; -.
DR eggNOG; arCOG01027; Archaea.
DR HOGENOM; CLU_041243_1_1_2; -.
DR InParanoid; Q58504; -.
DR OMA; CANRIPH; -.
DR OrthoDB; 91752at2157; -.
DR PhylomeDB; Q58504; -.
DR BioCyc; MetaCyc:MON-14633; -.
DR BRENDA; 2.7.1.39; 3260.
DR SABIO-RK; Q58504; -.
DR UniPathway; UPA00050; UER00064.
DR EvolutionaryTrace; Q58504; -.
DR Proteomes; UP000000805; 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; Reference proteome; Threonine biosynthesis;
KW Transferase.
FT CHAIN 1..296
FT /note="Homoserine kinase"
FT /id="PRO_0000156641"
FT BINDING 86..96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT STRAND 2..12
FT /evidence="ECO:0007829|PDB:1H72"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:1H72"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:1H72"
FT STRAND 21..47
FT /evidence="ECO:0007829|PDB:1H72"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:1H72"
FT HELIX 59..70
FT /evidence="ECO:0007829|PDB:1H72"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:1H72"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:1H72"
FT HELIX 93..108
FT /evidence="ECO:0007829|PDB:1H72"
FT HELIX 115..130
FT /evidence="ECO:0007829|PDB:1H72"
FT HELIX 138..143
FT /evidence="ECO:0007829|PDB:1H72"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:1H72"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:1H72"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:1H72"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:1H72"
FT HELIX 179..184
FT /evidence="ECO:0007829|PDB:1H72"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:1H74"
FT HELIX 192..210
FT /evidence="ECO:0007829|PDB:1H72"
FT HELIX 214..221
FT /evidence="ECO:0007829|PDB:1H72"
FT HELIX 228..232
FT /evidence="ECO:0007829|PDB:1H72"
FT HELIX 238..245
FT /evidence="ECO:0007829|PDB:1H72"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:1H72"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:1H72"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:1H72"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:1H72"
FT HELIX 270..280
FT /evidence="ECO:0007829|PDB:1H72"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:1H72"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:1H74"
SQ SEQUENCE 296 AA; 32259 MW; 49919E68F3834C78 CRC64;
MKVRVKAPCT SANLGVGFDV FGLCLKEPYD VIEVEAIDDK EIIIEVDDKN IPTDPDKNVA
GIVAKKMIDD FNIGKGVKIT IKKGVKAGSG LGSSAASSAG TAYAINELFK LNLDKLKLVD
YASYGELASS GAKHADNVAP AIFGGFTMVT NYEPLEVLHI PIDFKLDILI AIPNISINTK
EAREILPKAV GLKDLVNNVG KACGMVYALY NKDKSLFGRY MMSDKVIEPV RGKLIPNYFK
IKEEVKDKVY GITISGSGPS IIAFPKEEFI DEVENILRDY YENTIRTEVG KGVEVV
