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Entry: D8IXA0_HERSS
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ID   D8IXA0_HERSS            Unreviewed;       318 AA.
AC   D8IXA0;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   19-FEB-2014, entry version 20.
DE   RecName: Full=Homoserine kinase;
DE            Short=HK;
DE            Short=HSK;
DE            EC=2.7.1.39;
GN   Name=thrB; OrderedLocusNames=Hsero_0450;
OS   Herbaspirillum seropedicae (strain SmR1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herbaspirillum.
OX   NCBI_TaxID=757424;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SmR1;
RA   Pedrosa F.O., Monteiro R.A., Wassem R., Cruz L.M., Ayub R.A.,
RA   Colauto N.B., Fernandez M.A., Fungaro M.H.P., Grisard E.C.,
RA   Hungria M., Madeira H.M.F., Nodari R.O., Osaku C.A., Petzl-Erler M.L.,
RA   Terenzi H., Vieira L.G.E., Almeida M.I.M., Alves L.R., Arantes O.M.N.,
RA   Balsanelli E., Barcellos F.G., Baura V.A., Binde D.R., Campo R.J.,
RA   Chubatsu L.S., Chueire L.M.O., Ciferri R.R., Correa L.C.,
RA   da Conceicao Silva J.L., Dabul A.N.G., Dambros B.P., Faoro H.,
RA   Favetti A., Friedermann G., Furlaneto M.C., Gasques L.S.,
RA   Gimenes C.C.T., Gioppo N.M.R., Glienke-Blanco C., Godoy L.P.,
RA   Guerra M.P., Karp S., Kava-Cordeiro V., Margarido V.P., Mathioni S.M.,
RA   Menck-Soares M.A., Murace N.K., Nicolas M.F., Oliveira C.E.C.,
RA   Pagnan N.A.B., Pamphile J.A., Patussi E.V., Pereira L.F.P.,
RA   Pereira-Ferrari L., Pinto F.G.S., Precoma C., Prioli A.J.,
RA   Prioli S.M.A.P., Raittz R.T., Ramos H.J.O., Ribeiro E.M.S.F.,
RA   Rigo L.U., Rocha C.L.M.S.C., Rocha S.N., Santos K., Satori D.,
RA   Silva A.G., Simao R.C.G., Soares M.A.M., Souza E.M., Steffens M.B.R.,
RA   Steindel M., Tadra-Sfeir M.Z., Takahashi E.K., Torres R.A.,
RA   Valle J.S., Vernal J.I., Vilas-Boas L.A., Watanabe M.A.E., Weiss V.A.,
RA   Yates M.A., Souza E.M.;
RT   "The genome of Herbaspirillum seropedicae SmR1, an endophytic,
RT   nitrogen-fixing, plant-growth promoting beta-Proteobacteria.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + L-homoserine = ADP + O-phospho-L-
CC       homoserine.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 4/5.
CC   -!- SIMILARITY: Belongs to the pseudomonas-type ThrB family.
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DR   EMBL; CP002039; ADJ61975.1; -; Genomic_DNA.
DR   RefSeq; YP_003773883.1; NC_014323.1.
DR   ProteinModelPortal; D8IXA0; -.
DR   EnsemblBacteria; ADJ61975; ADJ61975; Hsero_0450.
DR   GeneID; 9401051; -.
DR   KEGG; hse:Hsero_0450; -.
DR   PATRIC; 42359573; VBIHerSer153339_0460.
DR   HOGENOM; HOG000004810; -.
DR   KO; K02204; -.
DR   BioCyc; HSER757424:GCTT-450-MONOMER; -.
DR   UniPathway; UPA00050; UER00064.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004413; F:homoserine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00301; Homoser_kinase_2; 1.
DR   InterPro; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR005280; Homoserine_kinase_ThrB.
DR   InterPro; IPR011009; Kinase-like_dom.
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; Complete proteome; Kinase;
KW   Nucleotide-binding; Threonine biosynthesis; Transferase.
SQ   SEQUENCE   318 AA;  35785 MW;  C9231442434CD1E6 CRC64;
     MAVFTPVSLE QLSDWLKHFP LGTATSIKGI SSGIENSNFF IGTERGEYVL TLFEKLHIEQ
     LPFYLELMRH LAERGIPVPA PVANDKGAIV SLLNDKPAAI VSKLEGQSQL DPQPVHCAAL
     GDMLARMHLA AKDFKILQPN LRGLAWWLET TPTVLPFLPA ELGRLLADEV QYQKDFAATA
     DYRALPRGPV HADLFRNNAM FVGERLSGIF DFYFAGCDTW LFDLAVTVND WCVDLDTGVL
     DLARTEAMLA AYRAVRPFSE AERIAWQPML RAAALRFWLS RLYDFYMPRA AEMLTPHDPT
     HFERILRLRI AETPPALS
//
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