ID A0A0A3VY57_9GAMM Unreviewed; 315 AA.
AC A0A0A3VY57;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=GW12_29130 {ECO:0000313|EMBL:KGT46052.1};
OS Acinetobacter sp. HR7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1509403 {ECO:0000313|EMBL:KGT46052.1, ECO:0000313|Proteomes:UP000032870};
RN [1] {ECO:0000313|EMBL:KGT46052.1, ECO:0000313|Proteomes:UP000032870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR7 {ECO:0000313|EMBL:KGT46052.1,
RC ECO:0000313|Proteomes:UP000032870};
RA Ahn S., Kim B.-C.;
RT "Genome sequencing of Acinetobacter sp. strain HR7.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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:KGT46052.1}.
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DR EMBL; JPQO01000226; KGT46052.1; -; Genomic_DNA.
DR RefSeq; WP_034589152.1; NZ_JPQO01000226.1.
DR AlphaFoldDB; A0A0A3VY57; -.
DR STRING; 1509403.GW12_29130; -.
DR PATRIC; fig|1509403.3.peg.2893; -.
DR eggNOG; COG2334; Bacteria.
DR OrthoDB; 9777460at2; -.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000032870; 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 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:KGT46052.1};
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:KGT46052.1}.
FT DOMAIN 26..254
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
SQ SEQUENCE 315 AA; 35342 MW; 861F83738D6116C1 CRC64;
MSVYTTLTLK EVQDFAAPYG LKAIDLIPIQ GGIQNTNYFL VCEDQQYVLT VFEDMDEQAA
GELVPVLEHL GKAGVAVPVP LSHSGKAIHS IKGKPAQIAP RLMGEHPMPA TTAQCEAIAI
AQAKIHVALQ DFHLEREFVR DHAYWYNVAQ EVKPTLNAAD KVLLGKLLGL YEALTAVYTD
RPRGFIHSDL FRDNTLFEGD ELKGILDFYE LNKDEFLFDI AITLNDFCTD YPAVTLNEER
AVAFLKAYET VRPLTEDEKA CLQLYLAMAA GRFWMMRLQV AQKNAAEGRT GADILQKNPE
EMRNMLIERL KFVTA
//