KHSE_CORGL
ID KHSE_CORGL Reviewed; 309 AA.
AC P07128; P08210;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Homoserine kinase;
DE Short=HK;
DE Short=HSK;
DE EC=2.7.1.39;
GN Name=thrB; OrderedLocusNames=Cgl1184, cg1338;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11.
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RX PubMed=2835591; DOI=10.1111/j.1365-2958.1988.tb00007.x;
RA Peoples O.P., Liebl W., Bodis M., Maeng P.J., Follettie M.T.,
RA Archer J.A.C., Sinskey A.J.;
RT "Nucleotide sequence and fine structural analysis of the Corynebacterium
RT glutamicum hom-thrB operon.";
RL Mol. Microbiol. 2:63-72(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13869 / DSMZ 1412 / NCIMB 9567;
RX PubMed=3035505; DOI=10.1093/nar/15.9.3922;
RA Mateos L.M., del Real G., Aguilar A., Martin J.F.;
RT "Nucleotide sequence of the homoserine kinase (thr B) gene of
RT Brevibacterium lactofermentum.";
RL Nucleic Acids Res. 15:3922-3922(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of L-homoserine
CC to L-homoserine phosphate. {ECO:0000250}.
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;
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 4/5.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase
CC subfamily. {ECO:0000305}.
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DR EMBL; Y00546; CAA68615.1; -; Genomic_DNA.
DR EMBL; Y00140; CAA68332.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB98577.1; -; Genomic_DNA.
DR EMBL; BX927151; CAF19888.1; -; Genomic_DNA.
DR PIR; S00866; KIFKMG.
DR RefSeq; NP_600410.1; NC_003450.3.
DR RefSeq; WP_011014183.1; NC_006958.1.
DR PDB; 5WAT; X-ray; 2.14 A; A/B=1-309.
DR PDBsum; 5WAT; -.
DR AlphaFoldDB; P07128; -.
DR SMR; P07128; -.
DR STRING; 196627.cg1338; -.
DR World-2DPAGE; 0001:P07128; -.
DR KEGG; cgb:cg1338; -.
DR KEGG; cgl:Cgl1184; -.
DR PATRIC; fig|196627.13.peg.1163; -.
DR eggNOG; COG0083; Bacteria.
DR HOGENOM; CLU_041243_0_1_11; -.
DR OMA; CANRIPH; -.
DR BRENDA; 2.7.1.39; 960.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000000582; Chromosome.
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; -; 1.
DR HAMAP; MF_00384; Homoser_kinase; 1.
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_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PIRSF; PIRSF000676; Homoser_kin; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
DR TIGRFAMs; TIGR00191; thrB; 1.
DR PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Kinase; Nucleotide-binding; Reference proteome;
KW Threonine biosynthesis; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2835591"
FT CHAIN 2..309
FT /note="Homoserine kinase"
FT /id="PRO_0000156565"
FT BINDING 95..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 246
FT /note="I -> V (in Ref. 2; CAA68332)"
FT /evidence="ECO:0000305"
FT STRAND 10..20
FT /evidence="ECO:0007829|PDB:5WAT"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:5WAT"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:5WAT"
FT STRAND 29..43
FT /evidence="ECO:0007829|PDB:5WAT"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:5WAT"
FT HELIX 65..78
FT /evidence="ECO:0007829|PDB:5WAT"
FT STRAND 84..92
FT /evidence="ECO:0007829|PDB:5WAT"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:5WAT"
FT HELIX 102..117
FT /evidence="ECO:0007829|PDB:5WAT"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:5WAT"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:5WAT"
FT HELIX 138..146
FT /evidence="ECO:0007829|PDB:5WAT"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:5WAT"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:5WAT"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:5WAT"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:5WAT"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:5WAT"
FT HELIX 203..221
FT /evidence="ECO:0007829|PDB:5WAT"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:5WAT"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:5WAT"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:5WAT"
FT HELIX 237..243
FT /evidence="ECO:0007829|PDB:5WAT"
FT HELIX 245..256
FT /evidence="ECO:0007829|PDB:5WAT"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:5WAT"
FT STRAND 270..276
FT /evidence="ECO:0007829|PDB:5WAT"
FT HELIX 280..288
FT /evidence="ECO:0007829|PDB:5WAT"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:5WAT"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:5WAT"
SQ SEQUENCE 309 AA; 32620 MW; 89C807BC983A60E7 CRC64;
MAIELNVGRK VTVTVPGSSA NLGPGFDTLG LALSVYDTVE VEIIPSGLEV EVFGEGQGEV
PLDGSHLVVK AIRAGLKAAD AEVPGLRVVC HNNIPQSRGL GSSAAAAVAG VAAANGLADF
PLTQEQIVQL SSAFEGHPDN AAASVLGGAV VSWTNLSIDG KSQPQYAAVP LEVQDNIRAT
ALVPNFHAST EAVRRVLPTE VTHIDARFNV SRVAVMIVAL QQRPDLLWEG TRDRLHQPYR
AEVLPITSEW VNRLRNRGYA AYLSGAGPTA MVLSTEPIPD KVLEDARESG IKVLELEVAG
PVKVEVNQP
