ID E4URC9_ARTGP Unreviewed; 546 AA.
AC E4URC9;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
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=MGYG_03196 {ECO:0000313|EMBL:EFR00192.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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}.
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DR EMBL; DS989823; EFR00192.1; -; Genomic_DNA.
DR RefSeq; XP_003175674.1; XM_003175626.1.
DR AlphaFoldDB; E4URC9; -.
DR STRING; 535722.E4URC9; -.
DR GeneID; 10030982; -.
DR VEuPathDB; FungiDB:MGYG_03196; -.
DR eggNOG; KOG4519; Eukaryota.
DR HOGENOM; CLU_022059_1_0_1; -.
DR InParanoid; E4URC9; -.
DR OMA; LVIHRTM; -.
DR OrthoDB; 991613at2759; -.
DR UniPathway; UPA00057; UER00099.
DR Proteomes; UP000002669; 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:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR016005; Erg8.
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; 3.
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:EFR00192.1};
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:UP000002669};
KW Steroid biosynthesis {ECO:0000256|PIRNR:PIRNR017288};
KW Steroid metabolism {ECO:0000256|ARBA:ARBA00023221,
KW ECO:0000256|PIRNR:PIRNR017288};
KW Sterol metabolism {ECO:0000256|ARBA:ARBA00023166};
KW Transferase {ECO:0000256|PIRNR:PIRNR017288}.
FT DOMAIN 252..314
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT REGION 98..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 546 AA; 58797 MW; 5722A109D2D34AA5 CRC64;
MDDAGSGLSH SRSVVLSPAE AASRHLELAR QRVVSFAAVS TRAAHTAKMI EQRQAATETA
VSAPGKVLLA GGYLVLDRDY TGTVCALDAR IHVVVQQQSV KRRPSATDTQ TEAPSQLSGG
QAAADGSSGS AENPPAIVNG GAQEEAVQDT VIVKSPQFVD AVWKYKIQRS DNGGGVRAVQ
CDDGPRNPFV ETSLNYALTY VSYVSASQNI GSLVVTILAD DDYYSETTAS STSDSSYAGF
KKFGVRLQDA HKTGLGSSAA LVTALVSALV VHRTVQPEKL SQNRAKLHNL AQAAHCAAQG
KIGSGFDVAA AVYGSCYYRR FSPSVLANLG EPGSPNFEDR LFAIVEDVDA SAPWDAECHD
IGFKLPMGIR MVLCDVDCGS QTPGMVKKLL RWRDENREEA DIIWANLQLN NEKIRLELKK
LLHSPGADFN ELRNLLLKSR MWIKTMTKKS EVPVEPMVQT ELLDSLGKLD GVIGGVVPGA
GGYDAIALLM IDDQDVYNDV CTHLKDWHST VEDDFGGKIE RVRLLGVGYG SEGILNELPV
RYSGWI
//
