ID A0A1B9G984_9TREE Unreviewed; 897 AA.
AC A0A1B9G984;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=mevalonate kinase {ECO:0000256|ARBA:ARBA00012103};
DE EC=2.7.1.36 {ECO:0000256|ARBA:ARBA00012103};
GN ORFNames=I302_02441 {ECO:0000313|EMBL:OCF27598.1};
OS Kwoniella bestiolae CBS 10118.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296100 {ECO:0000313|EMBL:OCF27598.1, ECO:0000313|Proteomes:UP000092730};
RN [1] {ECO:0000313|EMBL:OCF27598.1, ECO:0000313|Proteomes:UP000092730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10118 {ECO:0000313|EMBL:OCF27598.1,
RC ECO:0000313|Proteomes:UP000092730};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cryptococcus bestiolae CBS10118.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10118 {ECO:0000313|Proteomes:UP000092730};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+);
CC Xref=Rhea:RHEA:17065, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:36464, ChEBI:CHEBI:58146, ChEBI:CHEBI:456216;
CC EC=2.7.1.36; Evidence={ECO:0000256|ARBA:ARBA00029310};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17066;
CC Evidence={ECO:0000256|ARBA:ARBA00029310};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC step 1/3. {ECO:0000256|ARBA:ARBA00029438}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Mevalonate kinase
CC subfamily. {ECO:0000256|ARBA:ARBA00006495}.
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DR EMBL; KI894019; OCF27598.1; -; Genomic_DNA.
DR RefSeq; XP_019048668.1; XM_019189106.1.
DR AlphaFoldDB; A0A1B9G984; -.
DR STRING; 1296100.A0A1B9G984; -.
DR GeneID; 30206840; -.
DR VEuPathDB; FungiDB:I302_02441; -.
DR OrthoDB; 6018at2759; -.
DR UniPathway; UPA00057; UER00098.
DR Proteomes; UP000092730; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:InterPro.
DR GO; GO:0004496; F:mevalonate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:InterPro.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR CDD; cd00614; CGS_like; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.30.70.890; GHMP kinase, C-terminal domain; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR006238; Cys_b_lyase_euk.
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; IPR006205; Mev_gal_kin.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR01329; cysta_beta_ly_E; 1.
DR NCBIfam; TIGR00549; mevalon_kin; 1.
DR PANTHER; PTHR11808:SF50; CYSTATHIONINE BETA-LYASE; 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PRINTS; PR00959; MEVGALKINASE.
DR SUPFAM; SSF55060; GHMP Kinase, C-terminal domain; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
DR PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Lyase {ECO:0000313|EMBL:OCF27598.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000092730};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 597..673
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 759..816
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
FT REGION 845..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..870
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 897 AA; 95912 MW; F275685376795249 CRC64;
MTTPSTPGDS SLATSVYSLS SKSPTEAEQY KARAANWRFS TLCASVDNKD QYGASSTPIY
QTATFKGMDG QYDYTRSGNP TRGGLENHLA RLYGATQAFA LSTGMTCLDT ILRLVKPGET
VLAGDDLYGG TNRLLTYLGT HGGVKVIHAD TTRIEALRPY LQPGNKVRMV LLESPTNPLL
KIADLEGISK EVKQSSPDAL IVVDNTMMSP YLQRPLELGA DIVYDSGTKY LSGHHDLMAG
IIAVKRPEIC KDIAFLINSV GSGLAPFDSF LLLRGVKTMS LRMDRQMATA QLVALYLNSL
GFLVHYPGLK SHPKRDIHWK QATGAGAVLS FVTGDKALSE RIVGGTRLWG ISVSFGAVNS
LISMPCLMSH ASISAAVRAE RGLPENLIRL CVGIEDPRDL MDDLEHSLLS AGAITPNLSH
SPLSNSRSAE LYVSDPEAWI LERAKGFKRP SSESSAIDKL TIEEDIVVSA PGKVILFGEH
AVVHGVTAIA SSVNLRCFAV LSPRSDGKVA LEVPNVGVEA EWEISKLPWG LLPVHSNTHK
HVADKDLDPA LLQAIEKLVH EHKELGKTGI NSCIAYLYLY MVMAGAESEG PAVTFTATAN
LPISAGLGSS AAYSTCIASS LLIAHSHINK PNQDQTRLSE GETNIIDGWA FLSEKVLHGT
PSGIDNAVSV RGGAVAFTRA VGGRKGGLDG LHGFSSIRLL LTNTLVPRDT KSLVAGVSAK
RLAEPHVVDP ILDAIQSISD EASTLLSGQT QVERRDLITR LETLIRENHS HLVNLGVSHP
SLEMVVQATA AEPFGLATKL TGAGGGGCAV TLIPDDFPQS SLDALITTLE SQGFQPHLTS
VGGPGLGIHA SSSQKENKVR TSEEGEGMTV PKRVTLRETP IEGLQHWSER VGNWVHT
//
