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Database: UniProt/TrEMBL
Entry: A9IT64_BORPD
LinkDB: A9IT64_BORPD
Original site: A9IT64_BORPD 
ID   A9IT64_BORPD            Unreviewed;       322 AA.
AC   A9IT64;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   19-FEB-2014, entry version 46.
DE   RecName: Full=Homoserine kinase;
DE            Short=HK;
DE            Short=HSK;
DE            EC=2.7.1.39;
GN   Name=thrB; OrderedLocusNames=Bpet3045;
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448;
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P.,
RA   Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J.,
RA   Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N.,
RA   Larisch C., Link S., Linke B., Meyer F., Mormann S., Nakunst D.,
RA   Rueckert C., Schneiker-Bekel S., Schulze K., Voerholter F.-J.,
RA   Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B.,
RA   Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the
RT   metabolic versatility of environmental bacteria and virulence traits
RT   of pathogenic Bordetellae.";
RL   BMC Genomics 9:449-449(2008).
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; AM902716; CAP43387.1; -; Genomic_DNA.
DR   RefSeq; YP_001631655.1; NC_010170.1.
DR   ProteinModelPortal; A9IT64; -.
DR   STRING; 340100.Bpet3045; -.
DR   EnsemblBacteria; CAP43387; CAP43387; Bpet3045.
DR   GeneID; 5817468; -.
DR   KEGG; bpt:Bpet3045; -.
DR   PATRIC; 21167633; VBIBorPet31633_3070.
DR   eggNOG; COG2334; -.
DR   HOGENOM; HOG000004810; -.
DR   KO; K02204; -.
DR   OMA; FYNACSG; -.
DR   OrthoDB; EOG6BW4W1; -.
DR   ProtClustDB; PRK05231; -.
DR   BioCyc; BPET340100:GJBO-3080-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   322 AA;  35706 MW;  C152C6403FEC1910 CRC64;
     MAVFTPVSDD DARTLLAHFD LGDLVSLRGI TAGIENTNYF LATTRGEYVL TLFEVLTQAQ
     LPFYIELMHH LASRGVPVPQ PQTLRDGTRL TTLHGKPCAI VTRLPGGYEP APGPAHCALA
     GATLARAHLA ARDFPLQQPN LRGLAWWTAT APKVLPFLDA AQAQLLTSEL DEQQRVAATP
     LWQALPSGPA HCDLFRDNVL FAGTFEDPLM GGIIDFYFAG CDTWLFDVAV SVNDWCIERD
     SGVFVPALAQ SWLQAYAAVR PFTAGERQAW PAMLRAAALR FWLSRLYDYF LPRPAQTLKP
     HDPRHFERVL QARHRDDLPA LP
//
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