ID A0A1X1D9B4_9GAMM Unreviewed; 309 AA.
AC A0A1X1D9B4;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Homoserine kinase {ECO:0000256|ARBA:ARBA00017858, ECO:0000256|HAMAP-Rule:MF_00384};
DE Short=HK {ECO:0000256|HAMAP-Rule:MF_00384};
DE Short=HSK {ECO:0000256|HAMAP-Rule:MF_00384};
DE EC=2.7.1.39 {ECO:0000256|ARBA:ARBA00012078, ECO:0000256|HAMAP-Rule:MF_00384};
GN Name=thrB {ECO:0000256|HAMAP-Rule:MF_00384};
GN ORFNames=HA48_10445 {ECO:0000313|EMBL:ORM73283.1};
OS Pantoea wallisii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=1076551 {ECO:0000313|EMBL:ORM73283.1, ECO:0000313|Proteomes:UP000193104};
RN [1] {ECO:0000313|EMBL:ORM73283.1, ECO:0000313|Proteomes:UP000193104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 26277 {ECO:0000313|EMBL:ORM73283.1,
RC ECO:0000313|Proteomes:UP000193104};
RX PubMed=28255640;
RA Palmer M., Steenkamp E.T., Coetzee M.P., Chan W.Y., van Zyl E.,
RA De Maayer P., Coutinho T.A., Blom J., Smits T.H., Duffy B., Venter S.N.;
RT "Phylogenomic resolution of the bacterial genus Pantoea and its
RT relationship with Erwinia and Tatumella.";
RL Antonie Van Leeuwenhoek 0:0-0(2017).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of L-homoserine
CC to L-homoserine phosphate. {ECO:0000256|HAMAP-Rule:MF_00384}.
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|ARBA:ARBA00000528,
CC ECO:0000256|HAMAP-Rule:MF_00384};
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 4/5. {ECO:0000256|ARBA:ARBA00005015,
CC ECO:0000256|HAMAP-Rule:MF_00384}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00384}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase
CC subfamily. {ECO:0000256|ARBA:ARBA00007370, ECO:0000256|HAMAP-
CC Rule:MF_00384}.
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:ORM73283.1}.
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DR EMBL; MLFS01000024; ORM73283.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1D9B4; -.
DR STRING; 1076551.HA48_10445; -.
DR OrthoDB; 9769912at2; -.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000193104; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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 Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; GHMP kinase, C-terminal domain; 1.
DR HAMAP; MF_00384; Homoser_kinase; 1.
DR InterPro; IPR013750; GHMP_kinase_C_dom.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR006203; GHMP_knse_ATP-bd_CS.
DR InterPro; IPR000870; Homoserine_kinase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00191; thrB; 1.
DR PANTHER; PTHR20861:SF1; HOMOSERINE KINASE; 1.
DR PANTHER; PTHR20861; HOMOSERINE/4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL KINASE; 1.
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; SSF55060; GHMP Kinase, C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00384};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00384}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00384};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00384};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00384};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697, ECO:0000256|HAMAP-
KW Rule:MF_00384};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00384}.
FT DOMAIN 84..150
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 211..279
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
FT BINDING 91..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00384"
SQ SEQUENCE 309 AA; 32938 MW; 2416E323403800C3 CRC64;
MVKIYAPASI GNVSVGFDVL GAAVSPVDGT LLGDCVSVEA ADSFSLVNKG RFVSKLPAEP
KENIVYQCWE RFCQAIGKQV PVAMTLEKNM PIGSGLGSSA CSVVAGLMAM NEFCGKPLSD
TELLALMGEL EGRISGSVHY DNVAPCFLGG VQLMIEENGI ISQEVPCFDD WLWVMAYPGI
KVSTAEARAI LPAQYRKQDV IKHGRLLAGF IHACHTRQPA LAAKLMQDVV AEPYRTKLLP
GFADARKAAA DIGALACGIS GSGPTLFAVC NEMATAQRMA GWLSQHYLQN DEGFVHICRL
DTAGARKLG
//
