KHSE_GLUOX
ID KHSE_GLUOX Reviewed; 316 AA.
AC Q5FUH8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=GOX0178;
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H;
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(2005).
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; CP000009; AAW59968.1; -; Genomic_DNA.
DR RefSeq; WP_011251771.1; NZ_LT900338.1.
DR AlphaFoldDB; Q5FUH8; -.
DR SMR; Q5FUH8; -.
DR STRING; 290633.GOX0178; -.
DR PRIDE; Q5FUH8; -.
DR EnsemblBacteria; AAW59968; AAW59968; GOX0178.
DR KEGG; gox:GOX0178; -.
DR eggNOG; COG2334; Bacteria.
DR HOGENOM; CLU_053300_1_0_5; -.
DR OMA; DPTHFER; -.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000006375; 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..316
FT /note="Homoserine kinase"
FT /id="PRO_1000022581"
SQ SEQUENCE 316 AA; 34581 MW; EEACD0BBC94E4AFE CRC64;
MAVYTELAAE TLEAFLGTYD IGTLVSFHGI AEGVENSNFL LRTTEGDFIL TLFERRVNAR
ELPWFLGLMQ YLAGRGLNCP LPVSDRSGTA LRSLADRPAA ITTFLPGVSA TQLDANLCLE
LGKVLARLHI AGEGYDAVRP NALSPAAWGP LLDSCGESGD ELSPGLTAEV RKALQNVEAA
WPATADLPRG QIHADLFPDN VFFQNGQVSG LIDFYFACTD FLAYDLAICL NAWCFRDEKT
FEPSFAAAIM QGYESVRPLS DAEKAALPTL CQGAAIRFLL TRLYDWINTP ADALVTRKDP
LAYLRRLRHF QSASHV