KHSE_METRJ
ID KHSE_METRJ Reviewed; 321 AA.
AC B1M3E0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Homoserine kinase {ECO:0000255|HAMAP-Rule:MF_00301};
DE Short=HK {ECO:0000255|HAMAP-Rule:MF_00301};
DE Short=HSK {ECO:0000255|HAMAP-Rule:MF_00301};
DE EC=2.7.1.39 {ECO:0000255|HAMAP-Rule:MF_00301};
GN Name=thrB {ECO:0000255|HAMAP-Rule:MF_00301};
GN OrderedLocusNames=Mrad2831_4313;
OS Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 /
OS NBRC 15690 / NCIMB 10815 / 0-1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=426355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 / 0-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Marx C.J., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium radiotolerans JCM
RT 2831.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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_00301};
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00301}.
CC -!- SIMILARITY: Belongs to the pseudomonas-type ThrB family.
CC {ECO:0000255|HAMAP-Rule:MF_00301}.
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DR EMBL; CP001001; ACB26280.1; -; Genomic_DNA.
DR RefSeq; WP_012321234.1; NC_010505.1.
DR AlphaFoldDB; B1M3E0; -.
DR SMR; B1M3E0; -.
DR STRING; 426355.Mrad2831_4313; -.
DR EnsemblBacteria; ACB26280; ACB26280; Mrad2831_4313.
DR KEGG; mrd:Mrad2831_4313; -.
DR PATRIC; fig|426355.14.peg.4390; -.
DR eggNOG; COG2334; Bacteria.
DR HOGENOM; CLU_053300_1_0_5; -.
DR OMA; DPTHFER; -.
DR OrthoDB; 1003984at2; -.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000006589; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 CDD; cd05153; HomoserineK_II; 1.
DR HAMAP; MF_00301; Homoser_kinase_2; 1.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR005280; Homoserine_kinase_II.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR Pfam; PF01636; APH; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR TIGRFAMs; TIGR00938; thrB_alt; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; ATP-binding; Kinase; Nucleotide-binding;
KW Reference proteome; Threonine biosynthesis; Transferase.
FT CHAIN 1..321
FT /note="Homoserine kinase"
FT /id="PRO_1000115434"
SQ SEQUENCE 321 AA; 35192 MW; A9C4570E25A8DC21 CRC64;
MAVYTEVSDA ALAEFLSAYA IGSLLSFKGI AEGVENSNFF LHTTEGAYIL TLYEKRVREQ
DLPFFIGLME HLSARGLACP QPVRDRAGQA LGQLCGRPAA IVSFLEGVSV KAPGAEHCRE
LGRALAELHA AGRDFPMVRE NNLSVSAWRP LFAQAEAQAD SVEPGLAART RSDLAVLEAH
WPRDLPGGVI HADLFTDNVF FIGDALSGLI DFYFACTDAF AYDLAVCLNA WCFDPDGTFH
RDMAAALIAG YEAVRPLEAA EVAALPILCR GAALRFMLTR LVDWLNVPPG ALVKPKDPRE
FDRRLTFHRQ ARDARDYGRP H