ID A0A0S8D8C4_9PROT Unreviewed; 316 AA.
AC A0A0S8D8C4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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 ORFNames=AMJ66_06580 {ECO:0000313|EMBL:KPK32416.1};
OS Betaproteobacteria bacterium SG8_40.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1703389 {ECO:0000313|EMBL:KPK32416.1, ECO:0000313|Proteomes:UP000051602};
RN [1] {ECO:0000313|EMBL:KPK32416.1, ECO:0000313|Proteomes:UP000051602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_40 {ECO:0000313|EMBL:KPK32416.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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|ARBA:ARBA00038240, ECO:0000256|HAMAP-Rule:MF_00301}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPK32416.1}.
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DR EMBL; LJTS01000094; KPK32416.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8D8C4; -.
DR PATRIC; fig|1703389.3.peg.24; -.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000051602; Unassembled WGS sequence.
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:KPK32416.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00301};
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:KPK32416.1}.
FT DOMAIN 27..251
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
SQ SEQUENCE 316 AA; 35228 MW; A6A8E2D482A32343 CRC64;
MSVFTTVTPE QARAWLRNYS IGSLVELKGI LSGIENTNYF LTTAHGRYVL TLFEKLTPNE
LPFYLNLMAH LSNHGVPSPK PIANLQNEFL GELNGKPAAI VTCLPGQPVM DPGPDHCALV
GEQLADMHLS GQSFKQHLDN LRCANWWTRV APEIYPFLSQ DDAQLLQSEI EFQAAVSREG
LPRGPVHADL FRDNVLFDGD VVGGFIDFYF ACVDSLIYDV AITVNDWCAN PDATLDAERC
EAMLGAYATV RSFTDQERAL WPAMLRAGAL RFWVSRLYDF HLPRPGELTH AHDPEPFRRL
LQSHRNGGAD ASFLPG
//