ID W6PW31_PENRF Unreviewed; 353 AA.
AC W6PW31;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=homoserine kinase {ECO:0000256|ARBA:ARBA00012078};
DE EC=2.7.1.39 {ECO:0000256|ARBA:ARBA00012078};
GN Name=THR1 {ECO:0000313|EMBL:CDM28120.1};
GN ORFNames=PROQFM164_S01g001931 {ECO:0000313|EMBL:CDM28120.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM28120.1};
RN [1] {ECO:0000313|EMBL:CDM28120.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM28120.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 4/5. {ECO:0000256|ARBA:ARBA00005015}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase
CC subfamily. {ECO:0000256|ARBA:ARBA00007370}.
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DR EMBL; HG792015; CDM28120.1; -; Genomic_DNA.
DR AlphaFoldDB; W6PW31; -.
DR STRING; 1365484.W6PW31; -.
DR OMA; CANRIPH; -.
DR OrthoDB; 11319at2759; -.
DR UniPathway; UPA00050; UER00064.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004413; F:homoserine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
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};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CDM28120.1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023011};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Steroid biosynthesis {ECO:0000256|ARBA:ARBA00023011};
KW Steroid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW Sterol biosynthesis {ECO:0000256|ARBA:ARBA00023011};
KW Sterol metabolism {ECO:0000256|ARBA:ARBA00023166};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 92..153
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 266..327
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
SQ SEQUENCE 353 AA; 38005 MW; 8BE68C22421910DD CRC64;
MTSFVIKIPC SSANIGPGFD VIGLALSLYL DLHVTIEAKP SSQLPFNCAI TYEDQSKSVE
KISLDPEVNL ITRVALYVLR CHDQRAFPVE TKVHITNPIP LGRGLGSSGT AVVAGVMLGN
EVGKLGLSKE RLLDFCLMIE RHPDNVAASL FGGFVGTYLN ELKPEDVARK EIPLSEVLPA
PAGGVDTGIR PPAPPMAIGH YRKFNWAPEI KAIAIIPDFV VPTANARNVL PETYSRADVV
FNLQRAALLP AALGSSPPDP DMIFLAMQDK VHQPYRKTLI PGLTEILQFM TPATQPGLLG
ICLSGAGPTI LALATDNFTE IADRIIAQFA SNNISCQWKL LEPAQDGATV TYN
//
