ID Q7VZ53_BORPE Unreviewed; 328 AA.
AC Q7VZ53;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 132.
DE RecName: Full=Homoserine kinase {ECO:0000256|HAMAP-Rule:MF_00301};
DE Short=HK {ECO:0000256|HAMAP-Rule:MF_00301};
DE Short=HSK {ECO:0000256|HAMAP-Rule:MF_00301};
DE EC=2.7.1.39 {ECO:0000256|HAMAP-Rule:MF_00301};
GN Name=thrB {ECO:0000256|HAMAP-Rule:MF_00301,
GN ECO:0000313|EMBL:CAE41382.1};
GN OrderedLocusNames=BP1084 {ECO:0000313|EMBL:CAE41382.1};
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313 {ECO:0000313|EMBL:CAE41382.1, ECO:0000313|Proteomes:UP000002676};
RN [1] {ECO:0000313|Proteomes:UP000002676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251
RC {ECO:0000313|Proteomes:UP000002676};
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
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:0000256|HAMAP-Rule:MF_00301};
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 4/5. {ECO:0000256|HAMAP-Rule:MF_00301}.
CC -!- SIMILARITY: Belongs to the pseudomonas-type ThrB family.
CC {ECO:0000256|HAMAP-Rule:MF_00301}.
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DR EMBL; BX640414; CAE41382.1; -; Genomic_DNA.
DR RefSeq; NP_879866.1; NC_002929.2.
DR RefSeq; WP_003812707.1; NZ_CP039022.1.
DR AlphaFoldDB; Q7VZ53; -.
DR STRING; 257313.BP1084; -.
DR PaxDb; 257313-BP1084; -.
DR GeneID; 69601006; -.
DR KEGG; bpe:BP1084; -.
DR PATRIC; fig|257313.5.peg.1159; -.
DR eggNOG; COG2334; Bacteria.
DR HOGENOM; CLU_053300_0_0_4; -.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000002676; 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 Gene3D; 3.90.1200.10; -; 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 NCBIfam; TIGR00938; thrB_alt; 1.
DR PANTHER; PTHR21064:SF6; APH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR21064; UNCHARACTERIZED; 1.
DR Pfam; PF01636; APH; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00301}; ATP-binding {ECO:0000256|HAMAP-Rule:MF_00301};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00301, ECO:0000313|EMBL:CAE41382.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00301};
KW Reference proteome {ECO:0000313|Proteomes:UP000002676};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697, ECO:0000256|HAMAP-
KW Rule:MF_00301};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00301, ECO:0000313|EMBL:CAE41382.1}.
FT DOMAIN 27..262
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
SQ SEQUENCE 328 AA; 36763 MW; 2C77F2118FD5415D CRC64;
MAVFTSVSDQ DARTLLARFD LGDLVSLRGI TAGIENTNFF LNTTRGEYVL TLFEVLTQEQ
LPFYIELMYH LAARGIPVPQ PQTLRDGTRL TTLHGKPCAI VTRLPGGYEP APGPDHCRLA
GATLARAHLA GQDFPLRQPN LRGLPWWQAT APKVLPFLEP GQARLLEAEL ADQQAHAATA
LWQSLPSGPA HCDLFRDNVL FAGTFDDPLM GGFIDFYFAG CDTWLFDVAV SVNDWCIVRD
TGEFVPELVH GWLQAYAEVR PFTDAERQAW PVMLRAAALR FWLSRLYDFY LPRPAQTLKP
HDPRHFERVL QARHRHPAPD LPKSEAAA
//
