KHSE_BRUME
ID KHSE_BRUME Reviewed; 326 AA.
AC Q8YFR2;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 101.
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}; OrderedLocusNames=BMEI1458;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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; AE008917; AAL52639.1; -; Genomic_DNA.
DR PIR; AD3434; AD3434.
DR RefSeq; WP_004683140.1; NZ_GG703778.1.
DR AlphaFoldDB; Q8YFR2; -.
DR SMR; Q8YFR2; -.
DR STRING; 224914.BMEI1458; -.
DR EnsemblBacteria; AAL52639; AAL52639; BMEI1458.
DR GeneID; 29594311; -.
DR KEGG; bme:BMEI1458; -.
DR PATRIC; fig|224914.52.peg.2131; -.
DR eggNOG; COG2334; Bacteria.
DR OMA; DPTHFER; -.
DR PhylomeDB; Q8YFR2; -.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000000419; Chromosome I.
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 Threonine biosynthesis; Transferase.
FT CHAIN 1..326
FT /note="Homoserine kinase"
FT /id="PRO_0000172186"
SQ SEQUENCE 326 AA; 36630 MW; 0BE3E69B6AC11AF0 CRC64;
MAVYTDINEI ELGAFLRHYD IGTLTSYKGI AEGVENSNYL LHTSSGSFIL TLYEKRTNRE
DLPFFLGLMQ HLAKRGLECP QPVVRNDGAM IGQLAGRPAA IVTFLEGMWM RRPTVAHCEA
VGEGLAHMHL AGADFPMRRR NGLTLPDWRP LWNLSRKCAD TVERGLVAET EADLDFLEKN
WPADLPQGVI HADLFPDNAF FLGDRLSGFI DFYFACTDIL AYDVAVCLNA WCFEKDFSYN
RTKGAALLRG YTSVRPLSEA EANALLVLAR GAAVRFMLTR LYDWLTVPAG SFVVKKDPME
YVRRMRFHRQ IESGAEYGLE MQGVAA
