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Database: UniProt
Entry: A0A093XMC9_TALMA
LinkDB: A0A093XMC9_TALMA
Original site: A0A093XMC9_TALMA 
ID   A0A093XMC9_TALMA        Unreviewed;       469 AA.
AC   A0A093XMC9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Phosphomevalonate kinase {ECO:0000256|ARBA:ARBA00012958, ECO:0000256|PIRNR:PIRNR017288};
DE            EC=2.7.4.2 {ECO:0000256|ARBA:ARBA00012958, ECO:0000256|PIRNR:PIRNR017288};
GN   ORFNames=GQ26_0191360 {ECO:0000313|EMBL:KFX46403.1};
OS   Talaromyces marneffei PM1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX46403.1, ECO:0000313|Proteomes:UP000029285};
RN   [1] {ECO:0000313|EMBL:KFX46403.1, ECO:0000313|Proteomes:UP000029285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PM1 {ECO:0000313|EMBL:KFX46403.1,
RC   ECO:0000313|Proteomes:UP000029285};
RX   PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA   Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA   Lin X.;
RT   "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT   of Dimorphic Transition in Penicillium marneffei.";
RL   PLoS Genet. 10:e1004662-e1004662(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-5-phosphomevalonate + ATP = (R)-5-diphosphomevalonate +
CC         ADP; Xref=Rhea:RHEA:16341, ChEBI:CHEBI:30616, ChEBI:CHEBI:57557,
CC         ChEBI:CHEBI:58146, ChEBI:CHEBI:456216; EC=2.7.4.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00029326};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16342;
CC         Evidence={ECO:0000256|ARBA:ARBA00029326};
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC       step 2/3. {ECO:0000256|ARBA:ARBA00005017,
CC       ECO:0000256|PIRNR:PIRNR017288}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. Mevalonate kinase
CC       subfamily. {ECO:0000256|ARBA:ARBA00006495,
CC       ECO:0000256|PIRNR:PIRNR017288}.
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:KFX46403.1}.
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DR   EMBL; JPOX01000019; KFX46403.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093XMC9; -.
DR   eggNOG; KOG4519; Eukaryota.
DR   HOGENOM; CLU_022059_1_0_1; -.
DR   UniPathway; UPA00057; UER00099.
DR   Proteomes; UP000029285; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004631; F:phosphomevalonate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.890; GHMP kinase, C-terminal domain; 1.
DR   InterPro; IPR016005; Erg8.
DR   InterPro; IPR036554; GHMP_kinase_C_sf.
DR   InterPro; IPR006204; GHMP_kinase_N_dom.
DR   InterPro; IPR035102; Phosphomevalonate_kinase.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   PANTHER; PTHR31814; -; 1.
DR   PANTHER; PTHR31814:SF2; PHOSPHOMEVALONATE KINASE; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   PIRSF; PIRSF017288; PMK_GHMP_euk; 1.
DR   SUPFAM; SSF55060; GHMP Kinase, C-terminal domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|PIRNR:PIRNR017288, ECO:0000313|EMBL:KFX46403.1};
KW   Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR017288};
KW   Lipid metabolism {ECO:0000256|PIRNR:PIRNR017288};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Steroid biosynthesis {ECO:0000256|PIRNR:PIRNR017288};
KW   Steroid metabolism {ECO:0000256|ARBA:ARBA00023221,
KW   ECO:0000256|PIRNR:PIRNR017288};
KW   Sterol biosynthesis {ECO:0000256|ARBA:ARBA00023011};
KW   Sterol metabolism {ECO:0000256|ARBA:ARBA00023166};
KW   Transferase {ECO:0000256|PIRNR:PIRNR017288}.
FT   DOMAIN          163..225
FT                   /note="GHMP kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00288"
FT   REGION          50..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   469 AA;  51117 MW;  46217768200B0BA9 CRC64;
     MPVHPNATTA VSAPGKVLLT GGYLVLDRHY TGTVFALDAR IHAVVQQLQR DRKGSNQPAD
     SIEAPPTTDE AVESQPESVI VRSPQFIDAV WEYGVQRCEQ GGGVKVTQRN EGYVADSKDL
     GSLFVTILAD NDYYSDANQP ANINQRNRGA FRDFGVKLQD AHKTGLGSSA ALVTALVSAL
     VMHRTMHPDD LLAVRDKLHN LAQAAHCAAQ GKVGSGFDVG AAVFGSCSYR RFSPSILEGL
     GDAGSPGFEE RLFSTVEDLD SAHPWDTEFM DIGMKLPPGM QMVLCDVDCG SQTPSMVRKV
     LEWRKQNKEE ADQLWDSLQA NNEKLRQELR RNAGNRADPE TEAAVAAEVS KNARILIQRS
     RNLLKAMTEK SGVPIEPRVQ TELLDAVSAV DGVIGGVVPG AGGYDAVVLL IRDDIEVIQR
     LNRLFESYSS QVEDDFGGKI DRVRMLGVRH GSDGIKNEHN NLGNYLAWL
//
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