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Database: UniProt
Entry: C5S1U5_9PAST
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ID   C5S1U5_9PAST            Unreviewed;       315 AA.
AC   C5S1U5;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 78.
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=AM305_01584 {ECO:0000313|EMBL:EER47135.1};
OS   Actinobacillus minor NM305.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=637911 {ECO:0000313|EMBL:EER47135.1, ECO:0000313|Proteomes:UP000005532};
RN   [1] {ECO:0000313|EMBL:EER47135.1, ECO:0000313|Proteomes:UP000005532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NM305 {ECO:0000313|EMBL:EER47135.1,
RC   ECO:0000313|Proteomes:UP000005532};
RX   PubMed=19819087; DOI=10.1016/j.vetmic.2009.09.030;
RA   Arya G., Niven D.F.;
RT   "Production of haemolysins by strains of the Actinobacillus
RT   minor/"porcitonsillarum" complex.";
RL   Vet. Microbiol. 141:332-341(2010).
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:EER47135.1}.
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DR   EMBL; ACQL01000093; EER47135.1; -; Genomic_DNA.
DR   RefSeq; WP_005823915.1; NZ_ACQL01000093.1.
DR   AlphaFoldDB; C5S1U5; -.
DR   eggNOG; COG0083; Bacteria.
DR   OrthoDB; 9769912at2; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000005532; 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          89..156
FT                   /note="GHMP kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00288"
FT   DOMAIN          219..292
FT                   /note="GHMP kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08544"
FT   BINDING         97..107
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00384"
SQ   SEQUENCE   315 AA;  34713 MW;  06FB9B1BF477614E CRC64;
     MTLRIYAPAS SANLSVGFDS LGTAISPIDG SLLGDVVQIE ECDQPFELES VGYFVRKLPK
     EPQKNIVYQA YVLFSERLKL RGGLVKNLRL TLEKNMPIGS GLGSSACSIV AALVALNKFH
     DEPFSKMELL EMMGELEGRI SGSIHYDNVA PCYLGGLQLM TQSLGNICQP IPFFDEWYWV
     LAYPGIEVST AEARAILPKS YTRQDMIAQS RYLGSFIHAC HTHQDVLAAT MMKDLIAEPY
     REALLPNFAE VRQGCKDLGA LAVGISGSGP TMFAIAPDLE HAQKLVAYLE KDYLQNNEGF
     IHICKVDNQG ARELK
//
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