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Database: UniProt/TrEMBL
Entry: A5D1T7_PELTS
LinkDB: A5D1T7_PELTS
Original site: A5D1T7_PELTS 
ID   A5D1T7_PELTS            Unreviewed;       300 AA.
AC   A5D1T7;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   29-MAY-2013, entry version 46.
DE   RecName: Full=Homoserine kinase;
DE            Short=HK;
DE            Short=HSK;
DE            EC=2.7.1.39;
GN   Name=ThrB; Synonyms=thrB; OrderedLocusNames=PTH_1600;
OS   Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Pelotomaculum.
OX   NCBI_TaxID=370438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13744 / JCM 10971 / SI;
RX   PubMed=18218977; DOI=10.1101/gr.7136508;
RA   Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT   "The genome of Pelotomaculum thermopropionicum reveals niche-
RT   associated evolution in anaerobic microbiota.";
RL   Genome Res. 18:442-448(2008).
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of L-
CC       homoserine to L-homoserine phosphate (By similarity).
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   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase
CC       subfamily.
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DR   EMBL; AP009389; BAF59781.1; -; Genomic_DNA.
DR   RefSeq; YP_001212150.1; NC_009454.1.
DR   ProteinModelPortal; A5D1T7; -.
DR   STRING; 370438.PTH_1600; -.
DR   EnsemblBacteria; BAF59781; BAF59781; PTH_1600.
DR   GeneID; 5138941; -.
DR   KEGG; pth:PTH_1600; -.
DR   PATRIC; 22910435; VBIPelThe8413_1809.
DR   eggNOG; COG0083; -.
DR   HOGENOM; HOG000247199; -.
DR   KO; K00872; -.
DR   OMA; LHEPYRW; -.
DR   ProtClustDB; CLSK853519; -.
DR   BioCyc; PTHE370438:GCGQ-1649-MONOMER; -.
DR   UniPathway; UPA00050; UER00064.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004413; F:homoserine kinase activity; IEA:HAMAP.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:HAMAP.
DR   Gene3D; 3.30.230.10; -; 1.
DR   HAMAP; MF_00384; Homoser_kinase; 1; -.
DR   InterPro; IPR013750; GHMP_kinase_C_dom.
DR   InterPro; IPR006204; GHMP_kinase_N_dom.
DR   InterPro; IPR000870; Homoserine_kinase.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   Pfam; PF08544; GHMP_kinases_C; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   PIRSF; PIRSF000676; Homoser_kin; 1.
DR   PRINTS; PR00958; HOMSERKINASE.
DR   SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1.
DR   TIGRFAMs; TIGR00191; thrB; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm;
KW   Kinase; Nucleotide-binding; Threonine biosynthesis; Transferase.
SQ   SEQUENCE   300 AA;  31193 MW;  FB5CBBB0CFD7C09A CRC64;
     MIRVQVPATS ANLGPGFDCL GMALELYNIV EMIPASRGLV IEVSGESAAD IPRDERNLVF
     QAAQRVFGNT GFSPPGLKLR LINQIPAARG LGSSTAAVVG GVVAANLLSG GKLGVKDMIN
     LASSIEGHPD NVAPAILGGI VVSVQMDGEV KCLKIQPPQG LKGVVAVPDF PLATRTAREI
     LPSQVPFQDA VFNLGRVALL VAALQQGDLS LLGPAMEDRL HQSLRSSLIP GLKKVLAAAK
     LAGARGVTLS GAGPAVIAFA DSNFDLIARV MSDTFRQNGV KSRVMVLKPS PVGVRAFEIK
//
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