ID I3UD69_ADVKW Unreviewed; 322 AA.
AC I3UD69;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=TKWG_14485 {ECO:0000313|EMBL:AFK62957.1};
OS Advenella kashmirensis (strain DSM 17095 / LMG 22695 / WT001)
OS (Tetrathiobacter kashmirensis).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae.
OX NCBI_TaxID=1036672 {ECO:0000313|EMBL:AFK62957.1, ECO:0000313|Proteomes:UP000005267};
RN [1] {ECO:0000313|EMBL:AFK62957.1, ECO:0000313|Proteomes:UP000005267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17095 / LMG 22695 / WT001
RC {ECO:0000313|Proteomes:UP000005267};
RX PubMed=21914874; DOI=10.1128/JB.05781-11;
RA Ghosh W., George A., Agarwal A., Raj P., Alam M., Pyne P., Das Gupta S.K.;
RT "Whole-genome shotgun sequencing of the sulfur-oxidizing chemoautotroph
RT Tetrathiobacter kashmirensis.";
RL J. Bacteriol. 193:5553-5554(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; CP003555; AFK62957.1; -; Genomic_DNA.
DR RefSeq; WP_014751048.1; NC_017964.1.
DR AlphaFoldDB; I3UD69; -.
DR STRING; 1036672.TKWG_14485; -.
DR KEGG; aka:TKWG_14485; -.
DR HOGENOM; CLU_053300_0_0_4; -.
DR OrthoDB; 9777460at2; -.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000005267; 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:AFK62957.1};
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:AFK62957.1}.
FT DOMAIN 27..262
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
SQ SEQUENCE 322 AA; 36554 MW; B0F5475F61F1587C CRC64;
MAVFTPITNQ EAAQFLGHYA LGEFVSLRGI TAGIENTNFF LNTTQGEYVL TVFEVLNHEQ
LNFYIELMHT LASKDVKVPM PQTQRDGKRI GTLKGKPAAI VDRLPGGYES DPGVQHCIIA
ARTQAQAHLA AKDFTLYQPN LRGLPWWEET YPAIRPFLTE SQNALFVSCL DEQRQVQQGN
DWKNMPAGAC HCDLFRDNVL FDGTYDDPRM GGIIDFYFAG HDAWLFDVAI AVNDWCIERS
TGALTPWLVQ AWLDAYAQER PFTETEKAMW PVALRAAALR FWASRLNDYF RPRPAQTLKP
HDPTHFERIL TLRVQQPAPP LP
//
