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Database: UniProt
Entry: D7DM77_METV0
LinkDB: D7DM77_METV0
Original site: D7DM77_METV0 
ID   D7DM77_METV0            Unreviewed;       320 AA.
AC   D7DM77;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 70.
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   OrderedLocusNames=M301_0402 {ECO:0000313|EMBL:ADI28788.1};
OS   Methylotenera versatilis (strain 301).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylotenera.
OX   NCBI_TaxID=666681 {ECO:0000313|EMBL:ADI28788.1, ECO:0000313|Proteomes:UP000000383};
RN   [1] {ECO:0000313|Proteomes:UP000000383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 {ECO:0000313|Proteomes:UP000000383};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Clum A., Land M., Hauser L., Kyrpides N., Ivanova N.,
RA   Chistoservova L., Kalyuzhnaya M., Woyke T.;
RT   "Complete sequence of Methylotenera sp. 301.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADI28788.1, ECO:0000313|Proteomes:UP000000383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 {ECO:0000313|EMBL:ADI28788.1,
RC   ECO:0000313|Proteomes:UP000000383};
RX   PubMed=21622745; DOI=10.1128/JB.00404-11;
RA   Lapidus A., Clum A., Labutti K., Kaluzhnaya M.G., Lim S., Beck D.A.,
RA   Glavina Del Rio T., Nolan M., Mavromatis K., Huntemann M., Lucas S.,
RA   Lidstrom M.E., Ivanova N., Chistoserdova L.;
RT   "Genomes of three methylotrophs from a single niche uncover genetic and
RT   metabolic divergence of Methylophilaceae.";
RL   J. Bacteriol. 193:3757-3764(2011).
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; CP002056; ADI28788.1; -; Genomic_DNA.
DR   RefSeq; WP_013147104.1; NC_014207.1.
DR   AlphaFoldDB; D7DM77; -.
DR   STRING; 666681.M301_0402; -.
DR   KEGG; meh:M301_0402; -.
DR   eggNOG; COG2334; Bacteria.
DR   HOGENOM; CLU_053300_0_0_4; -.
DR   OrthoDB; 9777460at2; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000000383; 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:ADI28788.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00301};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000383};
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:ADI28788.1}.
FT   DOMAIN          27..262
FT                   /note="Aminoglycoside phosphotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF01636"
SQ   SEQUENCE   320 AA;  35497 MW;  B0922ED674FBE2E8 CRC64;
     MSVFTSVSIP QLQTWLQDYA IGELVELKGI SSGITNTNYF VTTQHNGTQN KFVLTLFEHN
     TLEELPYFID LMSHLAAHGI PCPKPIADKS GNSLHMLNGK PAALISCLNG GDIEAPNVQQ
     CAAVGTVLAK MHIAGQSFEA EFPQHDSHNQ RGMDWRVKTA TQVLPHLPAA DQQLLNETLA
     FQAELDTAEL PMGVIHADLF RDNVLFDGNE IGGLIDFYYA CHDLLAYDLA IAVNDWCVNA
     DGSLDTPRLE AMFNAYQAVR PFTSAEHAAW PALLRIAALR FWLSRLYDQI YPQAGELTHA
     KDPNHFQRIL KLRTSLAKSK
//
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