ID A0A1V8TEA7_9PEZI Unreviewed; 455 AA.
AC A0A1V8TEA7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=B0A48_05106 {ECO:0000313|EMBL:OQO09703.1};
OS Rachicladosporium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQO09703.1, ECO:0000313|Proteomes:UP000192596};
RN [1] {ECO:0000313|Proteomes:UP000192596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:OQO09703.1}.
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DR EMBL; NAJO01000010; OQO09703.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8TEA7; -.
DR STRING; 1507870.A0A1V8TEA7; -.
DR InParanoid; A0A1V8TEA7; -.
DR OrthoDB; 991613at2759; -.
DR UniPathway; UPA00057; UER00099.
DR Proteomes; UP000192596; 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; IPR013750; GHMP_kinase_C_dom.
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; PF08544; GHMP_kinases_C; 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};
KW Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR017288};
KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR017288};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000192596};
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 158..223
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 346..410
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
SQ SEQUENCE 455 AA; 48989 MW; 93AFC4FFA6A5428F CRC64;
MADRQLVAVS APGKVLLAGG YLVLDRKHTG LVFGLDARIY CIVQEILTSS GVVLSEISVQ
SPQFENAVWH YGYRWDGRDG GMHMSELRRD ADLALSRNLF IETALCYALS YIGSVSSPII
APASITILAD NDYYSTPADL ESTDRFHNFG VPISKAHKTG LGSSAALVTA LTAAVLTHYL
PTALLDIRSD IGKRRLHNLA QAAHCAAQGK VGSGFDVASA VYGSCLYKRF SPDILSSHAE
PGAPGFASQL VATVDDIDSK WDTEITKAKV KVPEGLRLVM CDVSVGSQTP GMVKQVLAWR
KANQEEADWL WDDLQASNDA LAKELTVLAE ADAKVAPDYS RLRMCFSAIR ELIREMGEKS
EVSIEPPAQT KLLDACEAVE GVVGGTVPGA GGYDAIALLI QDKQSTVKAL KDLLEGWKFE
GEGVGGGKVS MLGVREEMEG VRVEDLSGYE SEYLQ
//
