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Database: UniProt
Entry: A0A094C1F5_9PEZI
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ID   A0A094C1F5_9PEZI        Unreviewed;       385 AA.
AC   A0A094C1F5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   08-NOV-2023, entry version 33.
DE   RecName: Full=Diphosphomevalonate decarboxylase {ECO:0000256|ARBA:ARBA00012296, ECO:0000256|PIRNR:PIRNR015950};
DE            EC=4.1.1.33 {ECO:0000256|ARBA:ARBA00012296, ECO:0000256|PIRNR:PIRNR015950};
GN   ORFNames=V492_01320 {ECO:0000313|EMBL:KFY16452.1};
OS   Pseudogymnoascus sp. VKM F-4246.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420902 {ECO:0000313|EMBL:KFY16452.1, ECO:0000313|Proteomes:UP000029299};
RN   [1] {ECO:0000313|EMBL:KFY16452.1, ECO:0000313|Proteomes:UP000029299}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY16452.1,
RC   ECO:0000313|Proteomes:UP000029299};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-5-diphosphomevalonate + ATP = ADP + CO2 + isopentenyl
CC         diphosphate + phosphate; Xref=Rhea:RHEA:23732, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57557,
CC         ChEBI:CHEBI:128769, ChEBI:CHEBI:456216; EC=4.1.1.33;
CC         Evidence={ECO:0000256|ARBA:ARBA00029323};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23733;
CC         Evidence={ECO:0000256|ARBA:ARBA00029323};
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC       step 3/3. {ECO:0000256|ARBA:ARBA00005055,
CC       ECO:0000256|RuleBase:RU363086}.
CC   -!- SIMILARITY: Belongs to the diphosphomevalonate decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00008831, ECO:0000256|PIRNR:PIRNR015950,
CC       ECO:0000256|RuleBase:RU363086}.
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:KFY16452.1}.
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DR   EMBL; JPJU01000337; KFY16452.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094C1F5; -.
DR   STRING; 1420902.A0A094C1F5; -.
DR   HOGENOM; CLU_040369_4_2_1; -.
DR   UniPathway; UPA00057; UER00100.
DR   Proteomes; UP000029299; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004163; F:diphosphomevalonate decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:UniProtKB-UniRule.
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; IPR036554; GHMP_kinase_C_sf.
DR   InterPro; IPR006204; GHMP_kinase_N_dom.
DR   InterPro; IPR005935; Mev_decarb.
DR   InterPro; IPR029765; Mev_diP_decarb.
DR   InterPro; IPR041431; Mvd1_C.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR01240; mevDPdecarb; 1.
DR   PANTHER; PTHR10977; DIPHOSPHOMEVALONATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR10977:SF3; DIPHOSPHOMEVALONATE DECARBOXYLASE; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   Pfam; PF18376; MDD_C; 1.
DR   PIRSF; PIRSF015950; Mev_P_decrbx; 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, ECO:0000256|PIRNR:PIRNR015950};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW   ECO:0000256|RuleBase:RU363086};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|PIRNR:PIRNR015950};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR015950};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR015950};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029299};
KW   Steroid biosynthesis {ECO:0000256|ARBA:ARBA00022955,
KW   ECO:0000256|RuleBase:RU363086};
KW   Steroid metabolism {ECO:0000256|ARBA:ARBA00023221,
KW   ECO:0000256|RuleBase:RU363086};
KW   Sterol biosynthesis {ECO:0000256|ARBA:ARBA00023011,
KW   ECO:0000256|RuleBase:RU363086};
KW   Sterol metabolism {ECO:0000256|ARBA:ARBA00023166,
KW   ECO:0000256|RuleBase:RU363086}.
FT   DOMAIN          109..167
FT                   /note="GHMP kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00288"
FT   DOMAIN          198..377
FT                   /note="Mvd1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18376"
SQ   SEQUENCE   385 AA;  40710 MW;  D864C41C7600C9C3 CRC64;
     MADSTVYQAS TTAPVNIAVV KYWGKRDPKL NLPTNSSLSV TLSQSDLKTH TTAACSSTFG
     SEDSLLLNGS PQDVSGARTQ ACFRELRSLR AALEAADPSL PKLSTLTLKI VSENNFPTAA
     GLASSAAGFA ALVRAVADLY ELPASKTELS KIARQGSGSA CRSLFGGYVA WDMGTAVDGS
     DSQAVEVAPA SHWPNMRALI LVASAEKKGV SSTAGMQTTV ATSELAKHRV EVVVPKHMEQ
     MIKAVKDKDF ELFGKVTMVE SNSFHATCLD TFPPIFYLND TSRSAIRAVE AINEKAGKII
     AAYTFDAGPN CVIYFEEENM SAVAGAIKSV LGSIEGWEGK GADIKLSDAA HLDERTVKAL
     QEGLSRVILT GVGEGPISVK ESLLK
//
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